Atomistry » Copper » PDB 2pp8-2vr6 » 2qdv
Atomistry »
  Copper »
    PDB 2pp8-2vr6 »
      2qdv »

Copper in PDB 2qdv: Structure of the Cu(II) Form of the M51A Mutant of Amicyanin

Protein crystallography data

The structure of Structure of the Cu(II) Form of the M51A Mutant of Amicyanin, PDB code: 2qdv was solved by C.J.Carrell, J.K.Ma, Y.Wang, 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 / 0.89
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 28.360, 55.390, 27.010, 90.00, 94.82, 90.00
R / Rfree (%) 11 / 13.5

Copper Binding Sites:

The binding sites of Copper atom in the Structure of the Cu(II) Form of the M51A Mutant of Amicyanin (pdb code 2qdv). 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 the Cu(II) Form of the M51A Mutant of Amicyanin, PDB code: 2qdv:

Copper binding site 1 out of 1 in 2qdv

Go back to Copper Binding Sites List in 2qdv
Copper binding site 1 out of 1 in the Structure of the Cu(II) Form of the M51A 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 Cu(II) Form of the M51A Mutant of Amicyanin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1107

b:8.3
occ:1.00
ND1 A:HIS53 2.0 6.1 1.0
ND1 A:HIS95 2.1 7.5 1.0
SG A:CYS92 2.2 6.6 1.0
SD A:MET98 2.9 6.5 1.0
CE1 A:HIS53 2.9 7.3 1.0
CE1 A:HIS95 3.0 8.4 1.0
CG A:HIS53 3.1 5.6 1.0
CG A:HIS95 3.1 7.2 1.0
CB A:CYS92 3.2 5.1 1.0
CB A:HIS95 3.3 7.8 1.0
CB A:HIS53 3.5 5.6 1.0
CA A:HIS53 3.7 5.1 1.0
CE A:MET98 3.7 9.0 1.0
O A:PRO52 3.8 7.0 1.0
NE2 A:HIS53 4.1 8.2 1.0
CD2 A:HIS53 4.2 7.3 1.0
NE2 A:HIS95 4.2 8.4 1.0
CD2 A:HIS95 4.2 8.4 1.0
CG A:PRO94 4.3 9.7 1.0
N A:HIS95 4.4 6.3 1.0
CG A:MET98 4.4 6.6 1.0
CE A:MET28 4.4 16.7 0.4
CA A:HIS95 4.4 6.6 1.0
CA A:CYS92 4.6 4.9 1.0
N A:HIS53 4.6 5.2 1.0
C A:PRO52 4.6 5.6 1.0
N A:ASN54 4.7 4.9 1.0
O A:HIS95 4.7 6.7 1.0
C A:HIS53 4.8 5.0 1.0
CD A:PRO94 4.8 6.8 1.0
CB A:MET98 4.9 6.5 1.0

Reference:

J.K.Ma, Y.Wang, C.J.Carrell, F.S.Mathews, V.L.Davidson. A Single Methionine Residue Dictates the Kinetic Mechanism of Interprotein Electron Transfer From Methylamine Dehydrogenase to Amicyanin. Biochemistry V. 46 11137 2007.
ISSN: ISSN 0006-2960
PubMed: 17824674
DOI: 10.1021/BI7012307
Page generated: Wed Oct 28 14:21:32 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy