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Copper in PDB 5n8f: Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 1.

Enzymatic activity of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 1.

All present enzymatic activity of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 1.:
1.7.2.1;

Protein crystallography data

The structure of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 1., PDB code: 5n8f was solved by S.Horrell, D.Kekilli, M.Hough, R.Strange, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.98 / 1.38
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 96.130, 96.130, 96.130, 90.00, 90.00, 90.00
R / Rfree (%) 11.7 / 15.6

Copper Binding Sites:

The binding sites of Copper atom in the Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 1. (pdb code 5n8f). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 1., PDB code: 5n8f:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5n8f

Go back to Copper Binding Sites List in 5n8f
Copper binding site 1 out of 2 in the Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 1.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 1. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu501

b:9.2
occ:1.00
ND1 A:HIS95 2.0 8.5 1.0
ND1 A:HIS145 2.1 7.8 1.0
SG A:CYS136 2.2 7.8 1.0
SD A:MET150 2.5 8.9 1.0
CE1 A:HIS95 3.0 8.9 1.0
CE1 A:HIS145 3.0 8.5 1.0
CG A:HIS95 3.0 8.3 1.0
CG A:HIS145 3.1 7.7 1.0
CB A:CYS136 3.2 7.2 1.0
CE A:MET150 3.4 9.3 1.0
CB A:HIS95 3.4 8.0 1.0
CB A:HIS145 3.5 6.2 1.0
CA A:HIS95 3.8 6.9 1.0
CG A:MET150 3.9 8.0 1.0
NE2 A:HIS95 4.1 8.8 1.0
NE2 A:HIS145 4.1 8.7 1.0
CD2 A:HIS95 4.1 8.4 1.0
CD2 A:HIS145 4.2 8.2 1.0
O A:LEU94 4.3 9.9 1.0
CG A:PRO138 4.3 10.2 1.0
CB A:MET150 4.4 6.7 1.0
SD A:MET62 4.5 10.3 1.0
CA A:CYS136 4.6 5.9 1.0
N A:ASN96 4.7 7.5 1.0
CD A:PRO138 4.7 8.6 1.0
CA A:HIS145 4.8 6.1 1.0
C A:HIS95 4.9 7.0 1.0
N A:HIS95 4.9 7.4 1.0
CB A:MET62 4.9 9.0 1.0
C A:LEU94 5.0 8.8 1.0

Copper binding site 2 out of 2 in 5n8f

Go back to Copper Binding Sites List in 5n8f
Copper binding site 2 out of 2 in the Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 1.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Serial Cu Nitrite Reductase Structures at Elevated Cryogenic Temperature, 240K. Dataset 1. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu502

b:9.3
occ:1.00
O A:HOH801 2.0 34.0 1.0
NE2 A:HIS100 2.0 6.5 1.0
NE2 A:HIS135 2.1 7.8 1.0
O A:HOH820 2.1 18.8 1.0
CE1 A:HIS100 3.0 6.0 1.0
CD2 A:HIS135 3.0 8.3 1.0
CD2 A:HIS100 3.1 5.5 1.0
CE1 A:HIS135 3.1 7.7 1.0
OD2 A:ASP98 3.8 17.4 1.0
ND1 A:HIS100 4.1 5.5 1.0
O A:HOH718 4.2 25.6 1.0
ND1 A:HIS135 4.2 6.6 1.0
CG A:HIS100 4.2 4.8 1.0
CG A:HIS135 4.2 6.4 1.0
CG A:ASP98 4.3 11.8 1.0
OD1 A:ASP98 4.6 11.5 1.0
O A:HOH828 4.8 10.4 1.0

Reference:

K.Sen, S.Horrell, D.Kekilli, C.W.Yong, T.W.Keal, H.Atakisi, D.W.Moreau, R.E.Thorne, M.A.Hough, R.W.Strange. Active-Site Protein Dynamics and Solvent Accessibility in Native Achromobacter Cycloclastes Copper Nitrite Reductase. Iucrj V. 4 495 2017.
ISSN: ESSN 2052-2525
PubMed: 28875036
DOI: 10.1107/S2052252517007527
Page generated: Sun Dec 13 11:18:53 2020

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