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Copper in PDB 1sf3: Structure of the Reduced Form of the P94A Mutant of Amicyanin

Protein crystallography data

The structure of Structure of the Reduced Form of the P94A Mutant of Amicyanin, PDB code: 1sf3 was solved by C.J.Carrell, D.Sun, S.Jiang, V.L.Davidson, F.S.Mathews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.05
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 28.412, 55.557, 27.122, 90.00, 95.98, 90.00
R / Rfree (%) 11.7 / 14.7

Copper Binding Sites:

The binding sites of Copper atom in the Structure of the Reduced Form of the P94A Mutant of Amicyanin (pdb code 1sf3). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structure of the Reduced Form of the P94A Mutant of Amicyanin, PDB code: 1sf3:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1sf3

Go back to Copper Binding Sites List in 1sf3
Copper binding site 1 out of 2 in the Structure of the Reduced Form of the P94A 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 the Reduced Form of the P94A Mutant of Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu107

b:14.1
occ:0.58
CU A:CU1107 0.0 14.1 0.6
CU A:CU1107 1.4 14.2 0.4
ND1 A:HIS53 1.8 11.5 0.4
ND1 A:HIS53 1.9 11.0 0.6
SG A:CYS92 2.1 10.8 1.0
CG A:HIS53 2.8 10.8 0.4
CE1 A:HIS53 2.8 11.1 0.4
CG A:HIS53 2.9 10.3 0.6
CE1 A:HIS53 2.9 10.7 0.6
CB A:CYS92 3.0 8.5 1.0
SD A:MET98 3.0 12.5 1.0
ND1 A:HIS95 3.1 16.6 0.4
CB A:HIS53 3.2 9.9 0.4
CB A:HIS53 3.2 10.1 0.6
CD2 A:HIS95 3.3 17.3 0.6
O A:HOH351 3.3 16.4 0.4
CA A:HIS53 3.5 9.0 1.0
CE A:MET98 3.7 17.0 1.0
CB A:HIS95 3.8 14.3 0.6
NE2 A:HIS53 3.8 12.3 0.4
CG A:HIS95 3.8 15.2 0.6
CD2 A:HIS53 3.8 11.9 0.4
CG A:HIS95 3.9 15.0 0.4
CB A:HIS95 4.0 14.3 0.4
NE2 A:HIS53 4.0 11.4 0.6
CD2 A:HIS53 4.0 11.4 0.6
CE1 A:HIS95 4.1 17.5 0.4
O A:PRO52 4.1 13.7 1.0
N A:ASN54 4.3 8.4 1.0
CA A:CYS92 4.4 7.7 1.0
NE2 A:HIS95 4.5 16.7 0.6
CG A:MET98 4.5 11.4 1.0
C A:HIS53 4.5 8.3 1.0
N A:HIS53 4.6 9.5 1.0
N A:HIS95 4.6 13.0 0.4
N A:HIS95 4.6 13.0 0.6
C A:PRO52 4.8 11.6 1.0
CA A:HIS95 4.8 13.0 0.6
CA A:HIS95 4.8 13.0 0.4
O A:ASN54 4.8 7.9 1.0
O A:HIS95 4.9 12.6 0.4
O A:HIS95 4.9 13.2 0.6
CB A:MET98 4.9 9.9 1.0

Copper binding site 2 out of 2 in 1sf3

Go back to Copper Binding Sites List in 1sf3
Copper binding site 2 out of 2 in the Structure of the Reduced Form of the P94A Mutant of Amicyanin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of the Reduced Form of the P94A Mutant of Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu107

b:14.2
occ:0.42
CU A:CU1107 0.0 14.2 0.4
CU A:CU1107 1.4 14.1 0.6
ND1 A:HIS95 2.0 16.6 0.4
O A:HOH351 2.1 16.4 0.4
SG A:CYS92 2.1 10.8 1.0
CD2 A:HIS95 2.2 17.3 0.6
ND1 A:HIS53 2.2 11.5 0.4
ND1 A:HIS53 2.7 11.0 0.6
CE1 A:HIS95 2.9 17.5 0.4
CE1 A:HIS53 3.0 11.1 0.4
CG A:HIS95 3.0 15.2 0.6
CG A:HIS95 3.1 15.0 0.4
NE2 A:HIS95 3.3 16.7 0.6
CG A:HIS53 3.4 10.8 0.4
CB A:HIS95 3.4 14.3 0.6
O A:PRO52 3.5 13.7 1.0
CE1 A:HIS53 3.5 10.7 0.6
CB A:HIS95 3.5 14.3 0.4
CB A:CYS92 3.5 8.5 1.0
CG A:HIS53 3.6 10.3 0.6
CA A:HIS53 3.7 9.0 1.0
N A:HIS95 3.8 13.0 0.4
N A:HIS95 3.8 13.0 0.6
CB A:HIS53 3.8 9.9 0.4
CB A:ALA94 3.9 21.7 1.0
CB A:HIS53 3.9 10.1 0.6
SD A:MET98 3.9 12.5 1.0
NE2 A:HIS95 4.1 16.6 0.4
CD2 A:HIS95 4.2 15.9 0.4
NE2 A:HIS53 4.2 12.3 0.4
CA A:HIS95 4.2 13.0 0.6
CA A:HIS95 4.3 13.0 0.4
ND1 A:HIS95 4.3 15.6 0.6
CE1 A:HIS95 4.3 15.7 0.6
C A:PRO52 4.4 11.6 1.0
CD2 A:HIS53 4.4 11.9 0.4
C A:ALA94 4.4 14.2 1.0
N A:HIS53 4.5 9.5 1.0
CA A:ALA94 4.5 15.6 1.0
NE2 A:HIS53 4.6 11.4 0.6
N A:ALA94 4.6 11.5 1.0
CD2 A:HIS53 4.7 11.4 0.6
N A:ASN54 4.7 8.4 1.0
C A:HIS53 4.8 8.3 1.0
CA A:CYS92 4.8 7.7 1.0
O A:HIS95 4.9 12.6 0.4
CE A:MET98 5.0 17.0 1.0

Reference:

C.J.Carrell, D.Sun, S.Jiang, V.L.Davidson, F.S.Mathews. Structural Studies of Two Mutants of Amicyanin From Paracoccus Denitrificans That Stabilize the Reduced State of the Copper. Biochemistry V. 43 9372 2004.
ISSN: ISSN 0006-2960
PubMed: 15260480
DOI: 10.1021/BI049634Z
Page generated: Wed Oct 28 14:17:10 2020
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