Structure of PDB 2xxg Chain A

Receptor sequence

>2xxgA (length=334) Species: 85698 (Achromobacter xylosoxidans)

DADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKGT
TLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHSVDFHGATGALG
GAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGMSGTLMVL
PRDGLKDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDTV
QVMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHLI
GGHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNHN
LIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIP

3D structure

• PDB: 2xxg Identification of the Proton Channel to the Active Site Type 2 Cu Centre of Nitrite Reductase: Structural and Enzymatic Properties of the His254Phe and Asn90Ser Mutants
• Chain: A
• Resolution: 1.6 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): H88 D91 H93 H128 C129 H138 M143 H248 E272 T273 H299
• 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	A	H89 C130 H139 M144	H88 C129 H138 M143
BS02	CU	A	H94 H129	H93 H128
BS03	ZN	A	H165 D167	H164 D166

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:2xxg, PDBe:2xxg, PDBj:2xxg
• PDBsum: 2xxg
• PubMed: 19053252
• UniProt: O68601