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Copper in PDB 1rzc: X-Ray Analysis of Metal Substituted Human Carbonic Anhydrase II Derivatives

Enzymatic activity of X-Ray Analysis of Metal Substituted Human Carbonic Anhydrase II Derivatives

All present enzymatic activity of X-Ray Analysis of Metal Substituted Human Carbonic Anhydrase II Derivatives:
4.2.1.1;

Protein crystallography data

The structure of X-Ray Analysis of Metal Substituted Human Carbonic Anhydrase II Derivatives, PDB code: 1rzc was solved by K.Hakansson, A.Wehnert, A.Liljas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%) n/a / n/a

Copper Binding Sites:

The binding sites of Copper atom in the X-Ray Analysis of Metal Substituted Human Carbonic Anhydrase II Derivatives (pdb code 1rzc). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the X-Ray Analysis of Metal Substituted Human Carbonic Anhydrase II Derivatives, PDB code: 1rzc:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1rzc

Go back to Copper Binding Sites List in 1rzc
Copper binding site 1 out of 2 in the X-Ray Analysis of Metal Substituted Human Carbonic Anhydrase II Derivatives


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of X-Ray Analysis of Metal Substituted Human Carbonic Anhydrase II Derivatives within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu262

b:8.9
occ:1.00
ND1 A:HIS119 2.1 3.5 1.0
NE2 A:HIS96 2.2 3.8 1.0
O A:HOH263 2.3 7.5 1.0
NE2 A:HIS94 2.3 6.0 1.0
O2 A:OXY500 2.4 11.9 1.0
CE1 A:HIS119 3.0 4.9 1.0
CG A:HIS119 3.1 4.9 1.0
CD2 A:HIS96 3.1 2.4 1.0
CE1 A:HIS94 3.2 7.3 1.0
CE1 A:HIS96 3.2 4.0 1.0
O1 A:OXY500 3.3 12.4 1.0
CD2 A:HIS94 3.3 6.7 1.0
CB A:HIS119 3.5 3.2 1.0
OG1 A:THR199 3.7 3.3 1.0
OE1 A:GLU106 4.1 4.0 1.0
NE2 A:HIS119 4.2 3.9 1.0
CD2 A:HIS119 4.2 6.1 1.0
CG A:HIS96 4.2 2.0 1.0
ND1 A:HIS96 4.3 2.1 1.0
ND1 A:HIS94 4.3 6.7 1.0
CG A:HIS94 4.4 6.4 1.0
O A:HOH292 4.4 25.9 1.0
CD A:GLU106 5.0 5.6 1.0

Copper binding site 2 out of 2 in 1rzc

Go back to Copper Binding Sites List in 1rzc
Copper binding site 2 out of 2 in the X-Ray Analysis of Metal Substituted Human Carbonic Anhydrase II Derivatives


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of X-Ray Analysis of Metal Substituted Human Carbonic Anhydrase II Derivatives within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:12.1
occ:0.20
NE2 A:HIS4 2.5 15.0 0.5
NE2 A:HIS64 2.6 4.4 0.4
CE1 A:HIS64 2.6 5.6 0.4
CE1 A:HIS4 2.9 14.8 0.5
CD2 A:HIS4 3.7 16.7 0.5
ND1 A:HIS64 3.8 6.4 0.4
O A:HOH332 3.9 25.4 0.7
CD2 A:HIS64 3.9 6.2 0.4
ND1 A:HIS4 4.1 16.1 0.5
O A:ASN62 4.2 14.3 1.0
CD2 A:HIS64 4.5 15.7 0.6
NE1 A:TRP5 4.5 10.4 1.0
CG A:HIS64 4.5 7.1 0.4
CG A:HIS4 4.6 17.7 0.5
CZ2 A:TRP5 4.7 10.0 1.0
CE2 A:TRP5 4.8 11.4 1.0

Reference:

K.Hakansson, A.Wehnert, A.Liljas. X-Ray Analysis of Metal-Substituted Human Carbonic Anhydrase II Derivatives. Acta Crystallogr.,Sect.D V. 50 93 1994.
ISSN: ISSN 0907-4449
PubMed: 15299481
DOI: 10.1107/S0907444993008790
Page generated: Thu Sep 3 16:17:28 2020
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