Structure of PDB 2jfc Chain E Binding Site BS02

Receptor Information

>2jfc Chain E (length=335) Species: 85698 (Achromobacter xylosoxidans)

DADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKGT
TLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGATGALG
GAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGLSGTLMVL
PRDGLKDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDTV
QVMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHLI
GGHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNHN
LIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIPR

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: 2jfc Chain E Residue 1338

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2jfc The Structure of the met144Leu Mutant of Copper Nitrite Reductase from Alcaligenes Xylosoxidans Provides the First Glimpse of a Protein-Protein Complex with Azurin II.
• Resolution: 2.4 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 H139 L144 H249 E273 T274 H300
• Catalytic site (residue number reindexed from 1): H88 D91 H93 H128 C129 H138 L143 H248 E272 T273 H299
• 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:2jfc, PDBe:2jfc, PDBj:2jfc
• PDBsum: 2jfc
• PubMed: 17503096
• UniProt: O68601