Copper in PDB 4bed: Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units

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>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 32;

Binding sites:

The binding sites of Copper atom in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units (pdb code 4bed). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 32 binding sites of Copper where determined in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units, PDB code: 4bed:
Jump to Copper binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Copper binding site 1 out of 32 in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu9001 b:0.0 occ:1.00 CU1 A:CUO9001 0.0 0.0 1.0 O2 A:CUO9001 1.9 0.0 1.0 O1 A:CUO9001 1.9 0.0 1.0 NE2 A:HIS60 2.0 0.0 1.0 NE2 A:HIS42 2.2 0.0 1.0 NE2 A:HIS69 2.2 0.0 1.0 CE1 A:HIS60 2.5 0.0 1.0 CE1 A:HIS42 2.9 0.0 1.0 CE1 A:HIS69 3.1 0.0 1.0 CD2 A:HIS60 3.3 0.0 1.0 CD2 A:HIS69 3.4 0.0 1.0 CD2 A:HIS42 3.4 0.0 1.0 CU2 A:CUO9001 3.5 0.0 1.0 ND1 A:HIS60 3.8 0.0 1.0 CB A:CYS58 4.1 0.0 1.0 ND1 A:HIS42 4.1 0.0 1.0 CG A:HIS60 4.2 0.0 1.0 CD2 A:LEU197 4.2 0.0 1.0 SG A:CYS58 4.2 0.0 1.0 CE2 A:PHE65 4.3 0.0 1.0 CE2 A:PHE206 4.3 0.0 1.0 ND1 A:HIS69 4.3 0.0 1.0 CG A:HIS42 4.4 0.0 1.0 CZ A:PHE206 4.4 0.0 1.0 CG A:HIS69 4.5 0.0 1.0 NE2 A:HIS210 4.6 0.0 1.0 CZ A:PHE65 4.8 0.0 1.0 CZ3 A:TRP68 4.8 0.0 1.0 NE2 A:HIS183 4.9 0.0 1.0

Copper binding site 2 out of 32 in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu9001 b:0.0 occ:1.00 CU2 A:CUO9001 0.0 0.0 1.0 O2 A:CUO9001 1.9 0.0 1.0 O1 A:CUO9001 1.9 0.0 1.0 NE2 A:HIS210 2.2 0.0 1.0 NE2 A:HIS183 2.3 0.0 1.0 NE2 A:HIS179 2.3 0.0 1.0 CE1 A:HIS210 2.6 0.0 1.0 CD2 A:HIS179 3.1 0.0 1.0 CE1 A:HIS183 3.2 0.0 1.0 CD2 A:HIS183 3.2 0.0 1.0 CE1 A:HIS179 3.3 0.0 1.0 CU1 A:CUO9001 3.5 0.0 1.0 NE2 A:HIS69 3.5 0.0 1.0 CD2 A:HIS210 3.6 0.0 1.0 CD2 A:HIS69 3.6 0.0 1.0 CE2 A:PHE206 3.7 0.0 1.0 ND1 A:HIS210 3.9 0.0 1.0 CZ A:PHE206 4.1 0.0 1.0 CZ A:PHE65 4.2 0.0 1.0 CG A:HIS179 4.3 0.0 1.0 ND1 A:HIS183 4.3 0.0 1.0 CG A:HIS183 4.4 0.0 1.0 CG A:HIS210 4.4 0.0 1.0 ND1 A:HIS179 4.4 0.0 1.0 CE1 A:HIS69 4.5 0.0 1.0 NE2 A:HIS42 4.5 0.0 1.0 CD2 A:PHE206 4.5 0.0 1.0 NE2 A:HIS60 4.6 0.0 1.0 CG A:HIS69 4.7 0.0 1.0 CD2 A:HIS209 4.7 0.0 1.0 CE2 A:PHE65 4.7 0.0 1.0 NE2 A:HIS209 4.8 0.0 1.0

Copper binding site 3 out of 32 in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 3 of Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu9002 b:0.0 occ:1.00 CU1 A:CUO9002 0.0 0.0 1.0 O2 A:CUO9002 1.9 0.0 1.0 O1 A:CUO9002 1.9 0.0 1.0 NE2 A:HIS462 2.2 0.2 1.0 NE2 A:HIS491 2.2 0.0 1.0 NE2 A:HIS482 2.2 0.0 1.0 CE1 A:HIS462 2.8 0.2 1.0 CE1 A:HIS482 3.0 0.0 1.0 CE1 A:HIS491 3.1 0.0 1.0 SG A:CYS480 3.2 0.0 1.0 CD2 A:HIS462 3.3 0.2 1.0 CD2 A:HIS491 3.3 0.0 1.0 CD2 A:HIS482 3.3 0.0 1.0 CU2 A:CUO9002 3.5 0.0 1.0 ND1 A:HIS462 3.9 0.2 1.0 NE2 A:HIS633 4.1 0.0 1.0 CG A:HIS462 4.2 0.2 1.0 CZ A:PHE629 4.2 0.0 1.0 ND1 A:HIS482 4.2 0.0 1.0 CB A:CYS480 4.3 0.0 1.0 ND1 A:HIS491 4.3 0.0 1.0 CG A:HIS482 4.4 0.0 1.0 CG A:HIS491 4.4 0.0 1.0 CE1 A:PHE629 4.5 0.0 1.0 CE2 A:PHE487 4.5 0.0 1.0 CZ A:PHE487 4.7 0.0 1.0 NE2 A:HIS606 4.9 0.0 1.0 CE1 A:HIS633 4.9 0.0 1.0 NE2 A:HIS602 5.0 0.0 1.0 CD2 A:LEU763 5.0 0.0 1.0

Copper binding site 4 out of 32 in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 4 of Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu9002 b:0.0 occ:1.00 CU2 A:CUO9002 0.0 0.0 1.0 O2 A:CUO9002 1.9 0.0 1.0 O1 A:CUO9002 1.9 0.0 1.0 NE2 A:HIS606 2.1 0.0 1.0 NE2 A:HIS602 2.2 0.0 1.0 NE2 A:HIS633 2.4 0.0 1.0 CE1 A:HIS633 3.0 0.0 1.0 CE1 A:HIS606 3.0 0.0 1.0 CD2 A:HIS606 3.1 0.0 1.0 CD2 A:HIS602 3.2 0.0 1.0 CE1 A:HIS602 3.2 0.0 1.0 CD2 A:HIS633 3.4 0.0 1.0 CU1 A:CUO9002 3.5 0.0 1.0 CE1 A:PHE629 3.6 0.0 1.0 NE2 A:HIS491 3.9 0.0 1.0 CZ A:PHE629 3.9 0.0 1.0 ND1 A:HIS633 4.0 0.0 1.0 ND1 A:HIS606 4.1 0.0 1.0 CD2 A:HIS491 4.1 0.0 1.0 CG A:HIS606 4.2 0.0 1.0 CG A:HIS633 4.2 0.0 1.0 ND1 A:HIS602 4.3 0.0 1.0 CG A:HIS602 4.3 0.0 1.0 CE1 A:HIS462 4.4 0.2 1.0 CD1 A:PHE629 4.4 0.0 1.0 CD2 A:HIS632 4.7 0.0 1.0 NE2 A:HIS462 4.9 0.2 1.0 CE1 A:HIS491 4.9 0.0 1.0 CE2 A:PHE629 5.0 0.0 1.0 CD2 A:LEU763 5.0 0.0 1.0

Copper binding site 5 out of 32 in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 5 of Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu9003 b:0.0 occ:1.00 CU1 A:CUO9003 0.0 0.0 1.0 O2 A:CUO9003 1.9 0.0 1.0 O1 A:CUO9003 1.9 0.0 1.0 NE2 A:HIS876 2.2 0.0 1.0 NE2 A:HIS896 2.3 0.0 1.0 NE2 A:HIS905 2.5 0.0 1.0 CE1 A:HIS876 2.9 0.0 1.0 CE1 A:HIS896 3.1 0.0 1.0 SG A:CYS894 3.2 0.0 1.0 CD2 A:HIS876 3.2 0.0 1.0 CE1 A:HIS905 3.2 0.0 1.0 CD2 A:HIS896 3.3 0.0 1.0 CU2 A:CUO9003 3.5 0.0 1.0 CD2 A:HIS905 3.6 0.0 1.0 ND1 A:HIS876 4.0 0.0 1.0 CG A:HIS876 4.2 0.0 1.0 CD2 A:LEU1033 4.2 0.0 1.0 ND1 A:HIS896 4.3 0.0 1.0 NE2 A:HIS1046 4.4 0.0 1.0 CG A:HIS896 4.4 0.0 1.0 CB A:CYS894 4.4 0.0 1.0 ND1 A:HIS905 4.5 0.0 1.0 CE2 A:PHE901 4.5 0.0 1.0 CG A:HIS905 4.7 0.0 1.0 CE2 A:PHE1042 4.8 0.0 1.0 CD2 A:LEU1177 4.8 0.0 1.0 CZ A:PHE901 4.8 0.0 1.0 NE2 A:HIS1019 4.9 0.0 1.0 CZ A:PHE1042 4.9 0.0 1.0

Copper binding site 6 out of 32 in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 6 of Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu9003 b:0.0 occ:1.00 CU2 A:CUO9003 0.0 0.0 1.0 O2 A:CUO9003 1.9 0.0 1.0 O1 A:CUO9003 1.9 0.0 1.0 NE2 A:HIS1015 2.0 0.0 1.0 NE2 A:HIS1046 2.2 0.0 1.0 NE2 A:HIS1019 2.2 0.0 1.0 CE1 A:HIS1046 2.5 0.0 1.0 CE1 A:HIS1019 2.8 0.0 1.0 CD2 A:HIS1015 2.8 0.0 1.0 CE1 A:HIS1015 3.0 0.0 1.0 CD2 A:HIS1046 3.5 0.0 1.0 CU1 A:CUO9003 3.5 0.0 1.0 CD2 A:HIS1019 3.5 0.0 1.0 NE2 A:HIS905 3.6 0.0 1.0 ND1 A:HIS1046 3.7 0.0 1.0 CD2 A:HIS905 3.8 0.0 1.0 CG A:HIS1015 4.0 0.0 1.0 CE2 A:PHE1042 4.1 0.0 1.0 ND1 A:HIS1015 4.1 0.0 1.0 ND1 A:HIS1019 4.1 0.0 1.0 CG A:HIS1046 4.2 0.0 1.0 CZ A:PHE1042 4.4 0.0 1.0 CE1 A:HIS876 4.4 0.0 1.0 CG A:HIS1019 4.5 0.0 1.0 CE1 A:HIS905 4.6 0.0 1.0 NE2 A:HIS876 4.7 0.0 1.0 CD2 A:PHE1042 4.8 0.0 1.0 CZ A:PHE901 4.8 0.0 1.0 CD2 A:HIS1045 4.9 0.0 1.0 CG A:HIS905 5.0 0.0 1.0

Copper binding site 7 out of 32 in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 7 of Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu9004 b:0.0 occ:1.00 CU1 A:CUO9004 0.0 0.0 1.0 O2 A:CUO9004 1.9 0.0 1.0 O1 A:CUO9004 1.9 0.0 1.0 NE2 A:HIS1293 2.1 0.0 1.0 NE2 A:HIS1320 2.2 0.0 1.0 NE2 A:HIS1311 2.3 0.0 1.0 CE1 A:HIS1311 2.7 0.0 1.0 CE1 A:HIS1293 2.9 0.0 1.0 CE1 A:HIS1320 3.0 0.0 1.0 CD2 A:HIS1293 3.1 0.0 1.0 CD2 A:HIS1320 3.4 0.0 1.0 CU2 A:CUO9004 3.5 0.0 1.0 CD2 A:HIS1311 3.6 0.0 1.0 SG A:CYS1309 3.9 0.0 1.0 ND1 A:HIS1293 4.0 0.0 1.0 ND1 A:HIS1311 4.0 0.0 1.0 CG A:HIS1293 4.1 0.0 1.0 CB A:CYS1309 4.1 0.0 1.0 NE2 A:HIS1455 4.2 0.0 1.0 ND1 A:HIS1320 4.3 0.0 1.0 CE2 A:PHE1451 4.3 0.0 1.0 CG A:HIS1311 4.4 0.0 1.0 CZ A:PHE1451 4.5 0.0 1.0 CG A:HIS1320 4.5 0.0 1.0 CE1 A:PHE1316 4.5 0.0 1.0 CD2 A:LEU1442 4.7 0.0 1.0 CE1 A:HIS1455 4.9 0.0 1.0 NE2 A:HIS1424 5.0 0.0 1.0

Copper binding site 8 out of 32 in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 8 of Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu9004 b:0.0 occ:1.00 CU2 A:CUO9004 0.0 0.0 1.0 NE2 A:HIS1424 1.9 0.0 1.0 O2 A:CUO9004 1.9 0.0 1.0 O1 A:CUO9004 1.9 0.0 1.0 NE2 A:HIS1455 2.2 0.0 1.0 NE2 A:HIS1428 2.2 0.0 1.0 CE1 A:HIS1455 2.6 0.0 1.0 CD2 A:HIS1424 2.7 0.0 1.0 CE1 A:HIS1424 2.9 0.0 1.0 CE1 A:HIS1428 3.0 0.0 1.0 CD2 A:HIS1428 3.4 0.0 1.0 CD2 A:HIS1455 3.5 0.0 1.0 CU1 A:CUO9004 3.5 0.0 1.0 NE2 A:HIS1320 3.8 0.0 1.0 ND1 A:HIS1455 3.9 0.0 1.0 CG A:HIS1424 3.9 0.0 1.0 CD2 A:HIS1320 3.9 0.0 1.0 ND1 A:HIS1424 4.0 0.0 1.0 ND1 A:HIS1428 4.2 0.0 1.0 CE2 A:PHE1451 4.2 0.0 1.0 CG A:HIS1455 4.3 0.0 1.0 CG A:HIS1428 4.4 0.0 1.0 CZ A:PHE1451 4.5 0.0 1.0 CZ A:PHE1316 4.6 0.0 1.0 CE1 A:HIS1320 4.7 0.0 1.0 CE1 A:HIS1293 4.8 0.0 1.0 CG A:HIS1320 4.9 0.0 1.0 CD2 A:PHE1451 5.0 0.0 1.0 CE1 A:PHE1316 5.0 0.0 1.0 NE2 A:HIS1293 5.0 0.0 1.0

Copper binding site 9 out of 32 in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 9 of Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu9005 b:0.0 occ:1.00 CU1 B:CUO9005 0.0 0.0 1.0 O1 B:CUO9005 1.9 0.0 1.0 O2 B:CUO9005 2.0 0.0 1.0 NE2 B:HIS1705 2.0 0.0 1.0 NE2 B:HIS1725 2.1 0.0 1.0 NE2 B:HIS1734 2.2 0.0 1.0 CE1 B:HIS1725 2.5 0.0 1.0 CE1 B:HIS1705 3.0 0.0 1.0 CD2 B:HIS1705 3.1 0.0 1.0 CE1 B:HIS1734 3.1 0.0 1.0 CD2 B:HIS1725 3.3 0.0 1.0 CD2 B:HIS1734 3.4 0.0 1.0 CU2 B:CUO9005 3.5 0.0 1.0 ND1 B:HIS1725 3.7 0.0 1.0 CG B:HIS1725 4.1 0.0 1.0 ND1 B:HIS1705 4.2 0.0 1.0 CG B:HIS1705 4.2 0.0 1.0 NE2 B:HIS1878 4.2 0.0 1.0 ND1 B:HIS1734 4.3 0.0 1.0 CE2 B:PHE1730 4.4 0.0 1.0 CE2 B:PHE1874 4.4 0.0 1.0 CG B:HIS1734 4.5 0.0 1.0 CD1 B:LEU1865 4.5 0.0 1.0 CZ B:PHE1874 4.5 0.0 1.0 CD2 B:LEU2008 4.5 0.0 1.0 SG B:CYS1723 4.9 0.0 1.0 NE2 B:HIS1847 4.9 0.0 1.0 CZ B:PHE1730 4.9 0.0 1.0 CE1 B:HIS1878 5.0 0.0 1.0 NE2 B:HIS1851 5.0 0.0 1.0

Copper binding site 10 out of 32 in the Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 10 of Keyhole Limpet Hemocyanin (Klh): 9A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units within 5.0Å range: probe atom residue distance (Å) B Occ B:Cu9005 b:0.0 occ:1.00 CU2 B:CUO9005 0.0 0.0 1.0 O2 B:CUO9005 1.8 0.0 1.0 O1 B:CUO9005 1.9 0.0 1.0 NE2 B:HIS1847 2.0 0.0 1.0 NE2 B:HIS1851 2.1 0.0 1.0 NE2 B:HIS1878 2.3 0.0 1.0 CE1 B:HIS1851 2.7 0.0 1.0 CE1 B:HIS1847 2.9 0.0 1.0 CE1 B:HIS1878 2.9 0.0 1.0 CD2 B:HIS1847 3.0 0.0 1.0 CD2 B:HIS1878 3.3 0.0 1.0 CD2 B:HIS1851 3.4 0.0 1.0 CU1 B:CUO9005 3.5 0.0 1.0 CE2 B:PHE1874 3.9 0.0 1.0 NE2 B:HIS1734 3.9 0.0 1.0 CD2 B:HIS1734 4.0 0.0 1.0 ND1 B:HIS1851 4.0 0.0 1.0 ND1 B:HIS1878 4.0 0.0 1.0 ND1 B:HIS1847 4.1 0.0 1.0 CG B:HIS1847 4.1 0.0 1.0 CG B:HIS1878 4.2 0.0 1.0 CZ B:PHE1874 4.2 0.0 1.0 CG B:HIS1851 4.3 0.0 1.0 CD2 B:HIS1877 4.6 0.0 1.0 CD2 B:PHE1874 4.6 0.0 1.0 NE2 B:HIS1705 4.8 0.0 1.0 CZ B:PHE1730 4.8 0.0 1.0 CD2 B:LEU2008 4.9 0.0 1.0

C.Gatsogiannis, J.Markl. Keyhole Limpet Hemocyanin: 9-A Cryoem Structure and Molecular Model of the KLH1 Didecamer Reveal the Interfaces and Intricate Topology of the 160 Functional Units. J.Mol.Biol. V. 385 963 2009.
ISSN: ISSN 0022-2836
PubMed: 19013468
DOI: 10.1016/J.JMB.2008.10.080