Structure of PDB 1oe2 Chain A

Receptor sequence
>1oe2A (length=335) Species: 85698 (Achromobacter xylosoxidans) [Search protein sequence]
EDADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKG
TTLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVEFHGATGAL
GGAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGMSGTLMV
LPRDGLKDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDT
VQVMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHL
IGGHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNH
NLIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIP
3D structure
PDB1oe2 Atomic Resolution Structures of Native Copper Nitrite Reductase from Alcaligenes Xylosoxidans and the Active Site Mutant Asp92Glu
ChainA
Resolution1.12 Å
3D
structure
Catalytic site residues are labeled in the structure
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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).
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 H89 C130 H139 M144
BS02 CU A E92 H94 H129 E92 H94 H129
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1oe2, PDBe:1oe2, PDBj:1oe2
PDBsum1oe2
PubMed12691751
UniProtO68601

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