Structure of PDB 2bp0 Chain A Binding Site BS03

Receptor Information

>2bp0 Chain A (length=335) Species: 85698 (Achromobacter xylosoxidans)

DADKLPHTKVTLVAPPQVHPHEQASKTGPKVVEFTMTIEEKKMVIDDKGT
TLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGATGALG
GAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGLSGTLMVL
PRDGLKDPEGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDTV
QVMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHLI
GGHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNHN
LIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIPR

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: 2bp0 Chain A Residue 1339

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2bp0 High Resolution Structural Studies of Mutants Provide Insights Into Catalysis and Electron Transfer Processes in Copper Nitrite Reductase
• Resolution: 1.9 Å
• Binding residue (original residue number in PDB): H165 D167
• Binding residue (residue number reindexed from 1): H164 D166
• 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:2bp0, PDBe:2bp0, PDBj:2bp0
• PDBsum: 2bp0
• PubMed: 15927201
• UniProt: O68601