Structure of PDB 1gs6 Chain X Binding Site BS02

Receptor Information

>1gs6 Chain X (length=336) Species: 85698 (Achromobacter xylosoxidans)

QDADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKG
TTLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGATGAL
GGAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGASGTLMV
LPRDGLKDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDT
VQVMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHL
IGGHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNH
NLIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIPR

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: 1gs6 Chain X Residue 1338

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1gs6 Biochemical and Crystallographic Studies of the met144Ala, Asp92Asn and His254Phe Mutants of the Nitrite Reductase from Alcaligenes Xylosoxidans Provide Insight Into the Enzyme Mechanism.
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): H94 H129
• Binding residue (residue number reindexed from 1): H94 H129
• Annotation score: 1

Enzymatic activity

• 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:1gs6, PDBe:1gs6, PDBj:1gs6
• PDBsum: 1gs6
• PubMed: 11829502
• UniProt: O68601