Structure of PDB 2vw6 Chain A Binding Site BS02

Receptor Information

>2vw6 Chain A (length=333) Species: 85698 (Achromobacter xylosoxidans)

ADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKGTT
LQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGATGALGG
AKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGMSGTLMVLP
RDGLKDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDTVQ
VMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHLIG
GHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNHNL
IEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIP

Ligand information

• Ligand ID: CU
• InChI: InChI=1S/Cu/q+2
• InChIKey: JPVYNHNXODAKFH-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cu+2]
  CACTVS 3.341: [Cu++]
• Formula: Cu
• Name: COPPER (II) ION
• DrugBank: DB14552
• PDB chain: 2vw6 Chain A Residue 502

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2vw6 On-Line Optical and X-Ray Spectroscopies with Crystallography: An Integrated Approach for Determining Metalloprotein Structures in Functionally Well Defined States.
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): H94 H129
• Binding residue (residue number reindexed from 1): H92 H127
• Annotation score: 1

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).

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

External links

• PDB: RCSB:2vw6, PDBe:2vw6, PDBj:2vw6
• PDBsum: 2vw6
• PubMed: 18728313
• UniProt: O68601