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Copper in PDB 4p5s: Structure of Reduced W45Y Mutant of Amicyanin

Protein crystallography data

The structure of Structure of Reduced W45Y Mutant of Amicyanin, PDB code: 4p5s was solved by N.Sukumar, V.L.Davidson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.00 / 1.02
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 27.165, 56.646, 28.663, 90.00, 96.67, 90.00
R / Rfree (%) 13.4 / 15

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Reduced W45Y Mutant of Amicyanin (pdb code 4p5s). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Structure of Reduced W45Y Mutant of Amicyanin, PDB code: 4p5s:

Copper binding site 1 out of 1 in 4p5s

Go back to Copper Binding Sites List in 4p5s
Copper binding site 1 out of 1 in the Structure of Reduced W45Y Mutant of Amicyanin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Reduced W45Y Mutant of Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:7.0
occ:1.00
ND1 A:HIS53 1.9 7.3 1.0
SG A:CYS92 2.1 6.8 1.0
CE1 A:HIS53 2.9 6.8 1.0
CG A:HIS53 2.9 6.0 1.0
SD A:MET98 3.0 6.8 1.0
CB A:CYS92 3.0 5.8 1.0
CB A:HIS53 3.3 6.0 1.0
CA A:HIS53 3.4 6.2 1.0
CD2 A:HIS95 3.6 10.8 1.0
CE A:MET98 3.6 7.1 1.0
O A:PRO52 3.9 8.3 1.0
NE2 A:HIS53 4.0 7.0 1.0
CD2 A:HIS53 4.1 6.6 1.0
CB A:HIS95 4.1 7.6 1.0
N A:ASN54 4.2 5.9 1.0
CG A:HIS95 4.2 9.1 1.0
C A:HIS53 4.4 6.1 1.0
CA A:CYS92 4.4 5.8 1.0
N A:HIS53 4.5 6.2 1.0
CG A:MET98 4.5 7.3 1.0
C A:PRO52 4.6 7.1 1.0
O A:ASN54 4.7 5.7 1.0
CG A:PRO94 4.8 9.1 1.0
NE2 A:HIS95 4.8 12.9 1.0
CB A:MET98 4.9 6.8 1.0
N A:HIS95 5.0 6.9 1.0

Reference:

B.A.Dow, N.Sukumar, J.O.Matos, M.Choi, A.Schulte, S.A.Tatulian, V.L.Davidson. The Sole Tryptophan of Amicyanin Enhances Its Thermal Stability But Does Not Influence the Electronic Properties of the Type 1 Copper Site. Arch.Biochem.Biophys. V.-551 20 2014.
ISSN: ESSN 1096-0384
PubMed: 24704124
DOI: 10.1016/J.ABB.2014.03.010
Page generated: Sun Dec 13 11:15:34 2020

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