Structure of PDB 2jfc Chain F

Receptor sequence
>2jfcF (length=335) Species: 85698 (Achromobacter xylosoxidans) [Search protein sequence]
DADKLPHTKVTLVAPPQVHPHEQATKSGPKVVEFTMTIEEKKMVIDDKGT
TLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGATGALG
GAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGLSGTLMVL
PRDGLKDPQGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDTV
QVMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHLI
GGHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNHN
LIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIPR
3D structure
PDB2jfc The Structure of the met144Leu Mutant of Copper Nitrite Reductase from Alcaligenes Xylosoxidans Provides the First Glimpse of a Protein-Protein Complex with Azurin II.
ChainF
Resolution2.4 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 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).
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 F H89 C130 H139 H88 C129 H138
BS02 CU F H94 H129 H93 H128
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:2jfc, PDBe:2jfc, PDBj:2jfc
PDBsum2jfc
PubMed17503096
UniProtO68601

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