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Copper in PDB 5ofc: Cu Nitrite Reductase Serial Data at Varying Temperatures 190K 21.65MGY

Enzymatic activity of Cu Nitrite Reductase Serial Data at Varying Temperatures 190K 21.65MGY

All present enzymatic activity of Cu Nitrite Reductase Serial Data at Varying Temperatures 190K 21.65MGY:
1.7.2.1;

Protein crystallography data

The structure of Cu Nitrite Reductase Serial Data at Varying Temperatures 190K 21.65MGY, PDB code: 5ofc was solved by S.Horrell, D.Kekilli, R.W.Strange, M.A.Hough, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.49 / 1.68
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 95.012, 95.012, 95.012, 90.00, 90.00, 90.00
R / Rfree (%) 19.7 / 22.8

Copper Binding Sites:

The binding sites of Copper atom in the Cu Nitrite Reductase Serial Data at Varying Temperatures 190K 21.65MGY (pdb code 5ofc). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Cu Nitrite Reductase Serial Data at Varying Temperatures 190K 21.65MGY, PDB code: 5ofc:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5ofc

Go back to Copper Binding Sites List in 5ofc
Copper binding site 1 out of 2 in the Cu Nitrite Reductase Serial Data at Varying Temperatures 190K 21.65MGY


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Cu Nitrite Reductase Serial Data at Varying Temperatures 190K 21.65MGY within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu401

b:23.9
occ:1.00
ND1 A:HIS95 2.1 21.0 1.0
ND1 A:HIS145 2.1 23.8 1.0
SG A:CYS136 2.2 21.5 1.0
SD A:MET150 2.7 26.7 1.0
CE1 A:HIS95 3.0 23.9 1.0
CE1 A:HIS145 3.0 22.2 1.0
CG A:HIS95 3.1 20.9 1.0
CG A:HIS145 3.2 22.6 1.0
CB A:CYS136 3.2 20.4 1.0
CE A:MET150 3.4 24.6 1.0
CB A:HIS95 3.5 20.8 1.0
CB A:HIS145 3.6 22.3 1.0
CA A:HIS95 3.9 20.3 1.0
CG A:MET150 4.0 25.7 1.0
NE2 A:HIS95 4.1 21.1 1.0
NE2 A:HIS145 4.2 23.6 1.0
O A:LEU94 4.2 23.3 1.0
CD2 A:HIS95 4.2 22.0 1.0
CG A:PRO138 4.2 23.4 1.0
CD2 A:HIS145 4.3 24.5 1.0
CB A:MET150 4.5 21.8 1.0
SD A:MET62 4.6 30.2 1.0
CA A:CYS136 4.6 19.4 1.0
CD A:PRO138 4.7 21.7 1.0
N A:ASN96 4.7 17.8 1.0
CA A:HIS145 4.8 19.6 1.0
N A:HIS95 4.8 21.4 1.0
C A:HIS95 4.9 19.5 1.0
C A:LEU94 4.9 22.8 1.0

Copper binding site 2 out of 2 in 5ofc

Go back to Copper Binding Sites List in 5ofc
Copper binding site 2 out of 2 in the Cu Nitrite Reductase Serial Data at Varying Temperatures 190K 21.65MGY


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Cu Nitrite Reductase Serial Data at Varying Temperatures 190K 21.65MGY within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu402

b:19.4
occ:1.00
O A:HOH620 1.9 40.1 1.0
NE2 A:HIS135 2.0 17.1 1.0
NE2 A:HIS100 2.1 15.1 1.0
CE1 A:HIS100 2.9 16.3 1.0
CD2 A:HIS135 3.0 17.5 1.0
CE1 A:HIS135 3.0 18.8 1.0
CD2 A:HIS100 3.2 16.6 1.0
OD2 A:ASP98 3.8 31.7 1.0
ND1 A:HIS100 4.1 16.0 1.0
ND1 A:HIS135 4.2 17.6 1.0
CG A:HIS135 4.2 16.8 1.0
CG A:HIS100 4.2 15.9 1.0
CG A:ASP98 4.4 26.4 1.0
OD1 A:ASP98 4.7 27.7 1.0

Reference:

S.Horrell, D.Kekilli, K.Sen, R.L.Owen, F.S.N.Dworkowski, S.V.Antonyuk, T.W.Keal, C.W.Yong, R.R.Eady, S.S.Hasnain, R.W.Strange, M.A.Hough. Enzyme Catalysis Captured Using Multiple Structures From One Crystal at Varying Temperatures. Iucrj V. 5 283 2018.
ISSN: ESSN 2052-2525
PubMed: 29755744
DOI: 10.1107/S205225251800386X
Page generated: Sun Dec 13 11:19:25 2020

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