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Copper in PDB 1ll1: Hydroxo Bridge Met Form Hemocyanin From Limulus

Protein crystallography data

The structure of Hydroxo Bridge Met Form Hemocyanin From Limulus, PDB code: 1ll1 was solved by S.Liu, K.Magnus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.00 / 2.55
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 116.610, 116.610, 285.610, 90.00, 90.00, 120.00
R / Rfree (%) 16.7 / 23

Other elements in 1ll1:

The structure of Hydroxo Bridge Met Form Hemocyanin From Limulus also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Hydroxo Bridge Met Form Hemocyanin From Limulus (pdb code 1ll1). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Hydroxo Bridge Met Form Hemocyanin From Limulus, PDB code: 1ll1:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1ll1

Go back to Copper Binding Sites List in 1ll1
Copper binding site 1 out of 2 in the Hydroxo Bridge Met Form Hemocyanin From Limulus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Hydroxo Bridge Met Form Hemocyanin From Limulus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu629

b:25.1
occ:1.00
O A:HOH675 1.9 18.8 1.0
NE2 A:HIS324 2.0 17.6 1.0
O A:HOH730 2.1 49.5 1.0
NE2 A:HIS364 2.1 14.5 1.0
CE1 A:HIS324 2.5 9.6 1.0
NE2 A:HIS328 2.5 18.2 1.0
CE1 A:HIS364 2.9 12.0 1.0
CU A:CU630 3.1 24.4 1.0
CD2 A:HIS324 3.2 14.4 1.0
CD2 A:HIS364 3.3 9.1 1.0
CE1 A:HIS328 3.4 14.0 1.0
CD2 A:HIS328 3.4 13.9 1.0
ND1 A:HIS324 3.7 9.4 1.0
NE2 A:HIS204 3.8 11.1 1.0
CD2 A:HIS204 3.8 11.7 1.0
CG A:HIS324 4.1 8.1 1.0
ND1 A:HIS364 4.1 15.3 1.0
CE1 A:PHE49 4.2 10.7 1.0
CG A:HIS364 4.3 9.6 1.0
CE2 A:PHE360 4.4 13.4 1.0
ND1 A:HIS328 4.5 12.7 1.0
CG A:HIS328 4.5 16.1 1.0
CZ A:PHE360 4.6 11.9 1.0
NE2 A:HIS173 4.6 10.2 1.0
NE2 A:HIS177 4.7 20.5 1.0
CZ A:PHE49 4.7 11.2 1.0
CE1 A:HIS204 4.7 8.9 1.0
O A:HOH643 4.8 36.4 1.0
CE1 A:PHE200 4.8 12.0 1.0
CG A:HIS204 4.8 15.2 1.0
CE1 A:HIS177 4.9 16.6 1.0
CE1 A:HIS173 4.9 17.0 1.0
CZ A:PHE200 5.0 11.8 1.0

Copper binding site 2 out of 2 in 1ll1

Go back to Copper Binding Sites List in 1ll1
Copper binding site 2 out of 2 in the Hydroxo Bridge Met Form Hemocyanin From Limulus


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Hydroxo Bridge Met Form Hemocyanin From Limulus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu630

b:24.4
occ:1.00
NE2 A:HIS173 2.0 10.2 1.0
O A:HOH675 2.0 18.8 1.0
NE2 A:HIS177 2.0 20.5 1.0
O A:HOH730 2.1 49.5 1.0
NE2 A:HIS204 2.3 11.1 1.0
CE1 A:HIS173 2.9 17.0 1.0
CE1 A:HIS177 2.9 16.6 1.0
CD2 A:HIS173 3.1 15.7 1.0
CU A:CU629 3.1 25.1 1.0
CD2 A:HIS177 3.2 17.7 1.0
CD2 A:HIS204 3.2 11.7 1.0
CE1 A:HIS204 3.4 8.9 1.0
ND1 A:HIS173 4.0 18.3 1.0
ND1 A:HIS177 4.1 12.2 1.0
CG A:HIS173 4.1 13.2 1.0
CG A:HIS177 4.2 18.0 1.0
CG A:HIS204 4.4 15.2 1.0
ND1 A:HIS204 4.5 13.1 1.0
NE2 A:HIS364 4.5 14.5 1.0
CZ A:PHE360 4.6 11.9 1.0
CE2 A:PHE360 4.6 13.4 1.0
CE1 A:PHE49 4.6 10.7 1.0
NE2 A:HIS324 4.7 17.6 1.0
CZ A:PHE49 4.7 11.2 1.0
CE1 A:HIS324 4.8 9.6 1.0
NE2 A:HIS328 4.8 18.2 1.0

Reference:

S.Liu, H.Ton-That, K.Magnus. Crystallographic Studies of Hydroxo, Nitrosyl, Azido and Fluro Met Form Hemocyanin Subunit II From Limulus To Be Published.
Page generated: Wed Oct 28 14:15:39 2020
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