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Copper in PDB 1arm: Carboxypeptidase A with Zn Replaced By Hg

Enzymatic activity of Carboxypeptidase A with Zn Replaced By Hg

All present enzymatic activity of Carboxypeptidase A with Zn Replaced By Hg:
3.4.17.1;

Protein crystallography data

The structure of Carboxypeptidase A with Zn Replaced By Hg, PDB code: 1arm was solved by H.M.Greenblatt, H.Feinberg, P.A.Tucker, G.Shoham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.10 / 1.76
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.700, 60.320, 47.200, 90.00, 97.39, 90.00
R / Rfree (%) 14.6 / n/a

Copper Binding Sites:

The binding sites of Copper atom in the Carboxypeptidase A with Zn Replaced By Hg (pdb code 1arm). 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 Carboxypeptidase A with Zn Replaced By Hg, PDB code: 1arm:

Copper binding site 1 out of 1 in 1arm

Go back to Copper Binding Sites List in 1arm
Copper binding site 1 out of 1 in the Carboxypeptidase A with Zn Replaced By Hg


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Carboxypeptidase A with Zn Replaced By Hg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu315

b:15.3
occ:0.60
C3 A:TRS319 2.2 10.0 0.4
OE2 A:GLU270 2.5 24.5 1.0
C A:TRS319 2.8 6.7 0.4
O A:HOH320 2.8 10.2 0.6
C2 A:TRS319 2.9 13.1 0.4
CD A:GLU270 3.0 34.6 1.0
N A:TRS319 3.2 1.1 0.4
O3 A:TRS319 3.4 27.1 0.4
OE1 A:GLU270 3.5 23.3 1.0
O2 A:TRS319 3.8 9.1 0.4
CD1 A:ILE247 3.8 76.5 1.0
CG A:GLU270 3.9 19.7 1.0
C1 A:TRS319 4.3 13.5 0.4
O A:TYR198 4.3 14.5 1.0
O A:HOH427 4.4 38.6 0.5
O1 A:TRS319 4.8 66.3 0.4
OH A:TYR248 4.8 82.9 1.0
O A:HOH470 4.9 51.8 0.6
OG A:SER199 4.9 46.0 1.0

Reference:

H.M.Greenblatt, H.Feinberg, P.A.Tucker, G.Shoham. Carboxypeptidase A: Native, Zinc-Removed and Mercury-Replaced Forms. Acta Crystallogr.,Sect.D V. 54 289 1998.
ISSN: ISSN 0907-4449
PubMed: 9867434
DOI: 10.1107/S0907444997010445
Page generated: Wed Sep 2 21:34:19 2020
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