Structure of PDB 2bp0 Chain A

Receptor sequence
>2bp0A (length=335) Species: 85698 (Achromobacter xylosoxidans) [Search protein sequence]
DADKLPHTKVTLVAPPQVHPHEQASKTGPKVVEFTMTIEEKKMVIDDKGT
TLQAMTFNGSMPGPTLVVHEGDYVQLTLVNPATNAMPHNVDFHGATGALG
GAKLTNVNPGEQATLRFKADRSGTFVYHCAPEGMVPWHVVSGLSGTLMVL
PRDGLKDPEGKPLHYDRAYTIGEFDLYIPKGPDGKYKDYATLAESYGDTV
QVMRTLTPSHIVFNGKVGALTGANALTAKVGETVLLIHSQANRDTRPHLI
GGHGDWVWETGKFANPPQRDLETWFIRGGSAGAALYTFKQPGVYAYLNHN
LIEAFELGAAGHIKVEGKWNDDLMKQIKAPAPIPR
3D structure
PDB2bp0 High Resolution Structural Studies of Mutants Provide Insights Into Catalysis and Electron Transfer Processes in Copper Nitrite Reductase
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the 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
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 A H89 C130 H139 H88 C129 H138
BS02 CU A H94 H129 H93 H128
BS03 ZN A H165 D167 H164 D166
BS04 ZN A H70 D73 H69 D72
BS05 ZN A H8 E34 H7 E33
BS06 ZN A D4 H8 D3 H7
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:2bp0, PDBe:2bp0, PDBj:2bp0
PDBsum2bp0
PubMed15927201
UniProtO68601

[Back to BioLiP]