Structure of PDB 1oe2 Chain A Binding Site BS01

Receptor Information

>1oe2 Chain A (length=335) Species: 85698 (Achromobacter xylosoxidans)

EDADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKG
TTLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVEFHGATGAL
GGAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGMSGTLMV
LPRDGLKDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDT
VQVMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHL
IGGHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNH
NLIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIP

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: 1oe2 Chain A Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1oe2 Atomic Resolution Structures of Native Copper Nitrite Reductase from Alcaligenes Xylosoxidans and the Active Site Mutant Asp92Glu
• Resolution: 1.12 Å
• Binding residue (original residue number in PDB): H89 C130 H139 M144
• Binding residue (residue number reindexed from 1): H89 C130 H139 M144
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H89 E92 H94 H129 C130 H139 M144 H249 E273 T274 H300
• Catalytic site (residue number reindexed from 1): H89 E92 H94 H129 C130 H139 M144 H249 E273 T274 H300
• 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:1oe2, PDBe:1oe2, PDBj:1oe2
• PDBsum: 1oe2
• PubMed: 12691751
• UniProt: O68601