Structure of PDB 2vmj Chain A Binding Site BS01

Receptor Information

>2vmj Chain A (length=326) Species: 85698 (Achromobacter xylosoxidans)

DADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKGT
TLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGATGALG
GAKLTNVNPGEQATLRFKADRSGTFVYHCTPHPFMSGTLMVLPRDGLKDP
QGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDTVQVMRTLTP
SHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHLIGGHGDWVW
ETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNHNLIEAFELG
AAGHIKVEGKWNDDLMKQIKAPAPIP

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 2vmj Chain A Residue 1328

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2vmj The Importance of the Long Type 1 Copper-Binding Loop of Nitrite Reductase for Structure and Function.
• Resolution: 2.5 Å
• Binding residue (original residue number in PDB): H94 H129
• Binding residue (residue number reindexed from 1): H93 H128
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H89 D92 H94 H129 C130 M136 H241 E265 T266 H292
• Catalytic site (residue number reindexed from 1): H88 D91 H93 H128 C129 M135 H240 E264 T265 H291
• 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:2vmj, PDBe:2vmj, PDBj:2vmj
• PDBsum: 2vmj
• PubMed: 18491346
• UniProt: O68601