Structure of PDB 2xx0 Chain B

Receptor sequence

>2xx0B (length=336) Species: 85698 (Achromobacter xylosoxidans)

EDADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKG
TTLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHSVDFHGATGAL
GGAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGMSGTLMV
LPRDGLKDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDT
VQVMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHL
IGGFGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNH
NLIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIPR

3D structure

• PDB: 2xx0 Proton-Coupled Electron Transfer in the Catalytic Cycle of Alcaligenes Xylosoxidans Copper-Dependent Nitrite Reductase.
• Chain: B
• Resolution: 1.46 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H89 D92 H94 H129 C130 H139 M144 H249 E273 T274 H300
• Catalytic site (residue number reindexed from 1): H89 D92 H94 H129 C130 H139 M144 H249 E273 T274 H300
• Enzyme Commision number: 1.7.2.1: nitrite reductase (NO-forming).

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CU	B	H89 C130 H139 M144	H89 C130 H139 M144
BS02	CU	B	H94 H129	H94 H129
BS03	ZN	B	H94 H129	H94 H129
BS04	ZN	B	H165 D167	H165 D167

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:2xx0, PDBe:2xx0, PDBj:2xx0
• PDBsum: 2xx0
• PubMed: 21469743
• UniProt: O68601