Structure of PDB 1gs6 Chain X

Receptor sequence
>1gs6X (length=336) Species: 85698 (Achromobacter xylosoxidans) [Search protein sequence]
QDADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKG
TTLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGATGAL
GGAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGASGTLMV
LPRDGLKDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDT
VQVMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHL
IGGHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNH
NLIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIPR
3D structure
PDB1gs6 Biochemical and Crystallographic Studies of the met144Ala, Asp92Asn and His254Phe Mutants of the Nitrite Reductase from Alcaligenes Xylosoxidans Provide Insight Into the Enzyme Mechanism.
ChainX
Resolution2.2 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
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 X H89 C130 H139 H89 C130 H139
BS02 CU X H94 H129 H94 H129
BS03 MG X E260 I277 R278 S281 E260 I277 R278 S281
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1gs6, PDBe:1gs6, PDBj:1gs6
PDBsum1gs6
PubMed11829502
UniProtO68601

[Back to BioLiP]