Structure of PDB 2vm3 Chain A

Receptor sequence
>2vm3A (length=333) Species: 85698 (Achromobacter xylosoxidans) [Search protein sequence]
ADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKGTT
LQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGATGALGG
AKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGMSGTLMVLP
RDGLKDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDTVQ
VMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHLIG
GHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNHNL
IEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIP
3D structure
PDB2vm3 Crystallography with Online Optical and X-Ray Absorption Spectroscopies Demonstrates an Ordered Mechanism in Copper Nitrite Reductase.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H89 D92 H94 H129 C130 H139 M144 H249 E273 T274 H300
Catalytic site (residue number reindexed from 1) H87 D90 H92 H127 C128 H137 M142 H247 E271 T272 H298
Enzyme Commision number 1.7.2.1: nitrite reductase (NO-forming).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CU A H89 C130 H139 M144 H87 C128 H137 M142
BS02 CU A H94 H129 H92 H127
BS03 ZN A H165 D167 H163 D165
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
GO:0050421 nitrite reductase (NO-forming) activity
Biological Process
GO:0019333 denitrification pathway
GO:0042128 nitrate assimilation
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2vm3, PDBe:2vm3, PDBj:2vm3
PDBsum2vm3
PubMed18353369
UniProtO68601

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