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Copper in PDB 1lla: Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation

Protein crystallography data

The structure of Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation, PDB code: 1lla was solved by B.Hazes, W.G.J.Hol, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.18
Space group R 3 2
Cell size a, b, c (Å), α, β, γ (°) 117.002, 117.002, 117.002, 60.02, 60.02, 60.02
R / Rfree (%) 17.4 / n/a

Other elements in 1lla:

The structure of Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Sodium (Na) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation (pdb code 1lla). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation, PDB code: 1lla:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1lla

Go back to Copper Binding Sites List in 1lla
Copper binding site 1 out of 2 in the Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu629

b:10.9
occ:1.00
NE2 A:HIS204 1.9 3.9 1.0
NE2 A:HIS177 2.0 5.1 1.0
NE2 A:HIS173 2.1 3.9 1.0
CE1 A:HIS204 2.7 4.1 1.0
CE1 A:HIS177 2.9 5.1 1.0
CD2 A:HIS173 2.9 4.2 1.0
CD2 A:HIS177 3.0 7.3 1.0
CD2 A:HIS204 3.1 5.2 1.0
CE1 A:HIS173 3.1 5.5 1.0
ND1 A:HIS204 3.9 6.3 1.0
ND1 A:HIS177 4.0 3.9 1.0
CG A:HIS204 4.1 5.5 1.0
CG A:HIS173 4.1 4.2 1.0
ND1 A:HIS173 4.1 5.3 1.0
CG A:HIS177 4.1 5.7 1.0
CE A:MET207 4.3 7.9 1.0
CZ A:PHE360 4.5 3.8 1.0
CU A:CU630 4.6 9.3 1.0
CE1 A:PHE360 4.7 5.4 1.0
CE1 A:HIS364 4.9 2.2 1.0

Copper binding site 2 out of 2 in 1lla

Go back to Copper Binding Sites List in 1lla
Copper binding site 2 out of 2 in the Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 Angstroms Resolution: Clues For A Mechanism For Allosteric Regulation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu630

b:9.3
occ:1.00
NE2 A:HIS364 1.9 3.4 1.0
NE2 A:HIS328 2.1 6.6 1.0
NE2 A:HIS324 2.2 2.6 1.0
CE1 A:HIS364 2.6 2.2 1.0
CE1 A:HIS328 2.9 4.9 1.0
CD2 A:HIS324 3.0 2.0 1.0
CD2 A:HIS364 3.1 5.5 1.0
CE1 A:HIS324 3.1 6.7 1.0
CD2 A:HIS328 3.1 5.2 1.0
CE1 A:PHE360 3.7 5.4 1.0
ND1 A:HIS364 3.8 7.8 1.0
CG A:HIS364 4.0 4.6 1.0
ND1 A:HIS328 4.1 6.0 1.0
CG A:HIS324 4.2 2.9 1.0
ND1 A:HIS324 4.2 2.0 1.0
CG A:HIS328 4.2 3.3 1.0
CD1 A:TRP363 4.2 2.0 1.0
CZ A:PHE360 4.4 3.8 1.0
CD1 A:PHE360 4.4 4.8 1.0
CU A:CU629 4.6 10.9 1.0
NE2 A:HIS204 4.6 3.9 1.0
NE1 A:TRP363 4.7 4.2 1.0
CD2 A:HIS204 4.7 5.2 1.0
CE1 A:PHE49 4.8 6.2 1.0

Reference:

B.Hazes, K.A.Magnus, C.Bonaventura, J.Bonaventura, Z.Dauter, K.H.Kalk, W.G.Hol. Crystal Structure of Deoxygenated Limulus Polyphemus Subunit II Hemocyanin at 2.18 A Resolution: Clues For A Mechanism For Allosteric Regulation. Protein Sci. V. 2 597 1993.
ISSN: ISSN 0961-8368
PubMed: 8518732
Page generated: Mon Jul 14 00:04:20 2025

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