Structure of PDB 2bmq Chain A

Receptor sequence
>2bmqA (length=437) Species: 58226 (Comamonas sp. JS765) [Search protein sequence]
YQNLVSEAGLTQKLLIHGDKELFQHELKTIFARNWLFLTHDSLIPSPGDY
VKAKMGVDEVIVSRQNDGSVRAFLNVCRHRGKTLVHAEAGNAKGFVCGYH
GWGYGSNGELQSVPFEKELYGDAIKKKCLGLKEVPRIESFHGFIYGCFDA
EAPPLIDYLGDAAWYLEPTFKYSGGLELVGPPGKVVVKANWKSFAENFVG
DGYHVGWTHAAALRAGQSVFSSIAGNAKLPPEGAGLQMTSKYGSGMGVFW
GYYSGNFSADMIPDLMAFGAAKQEKLAKEIGDVRARIYRSFLNGTIFPNN
SFLTGSAAFRVWNPIDENTTEVWTYAFVEKDMPEDLKRRVADAVQRSIGP
AGFWESDDNENMETMSQNGKKYQSSNIDQIASLGFGKDVYGDECYPGVVG
KSAIGETSYRGFYRAYQAHISSSNWAEFENASRNWHI
3D structure
PDB2bmq Structural insight into the dioxygenation of nitroarene compounds: the crystal structure of nitrobenzene dioxygenase.
ChainA
Resolution1.55 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) H102 D203 H206 H211 D360
Catalytic site (residue number reindexed from 1) H100 D201 H204 H209 D358
Enzyme Commision number ?
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 FES A C79 H81 R82 C99 Y101 H102 W104 C77 H79 R80 C97 Y99 H100 W102
BS02 FE A H206 H211 D360 H204 H209 D358
BS03 NBZ A N199 F200 H206 N258 F293 N295 N197 F198 H204 N256 F291 N293
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:0051537 2 iron, 2 sulfur cluster binding
Biological Process
GO:0009056 catabolic process
GO:0044237 cellular metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2bmq, PDBe:2bmq, PDBj:2bmq
PDBsum2bmq
PubMed15854650
UniProtQ8RTL4

[Back to BioLiP]