Structure of PDB 2bmo Chain A

Receptor sequence
>2bmoA (length=437) Species: 58226 (Comamonas sp. JS765) [Search protein sequence]
YQNLVSEAGLTQKLLIHGDKELFQHELKTIFARNWLFLTHDSLIPSPGDY
VKAKMGVDEVIVSRQNDGSVRAFLNVCRHRGKTLVHAEAGNAKGFVCGYH
GWGYGSNGELQSVPFEKELYGDAIKKKCLGLKEVPRIESFHGFIYGCFDA
EAPPLIDYLGDAAWYLEPTFKYSGGLELVGPPGKVVVKANWKSFAENFVG
DGYHVGWTHAAALRAGQSVFSSIAGNAKLPPEGAGLQMTSKYGSGMGVFW
GYYSGNFSADMIPDLMAFGAAKQEKLAKEIGDVRARIYRSFLNGTIFPNN
SFLTGSAAFRVWNPIDENTTEVWTYAFVEKDMPEDLKRRVADAVQRSIGP
AGFWESDDNENMETMSQNGKKYQSSNIDQIASLGFGKDVYGDECYPGVVG
KSAIGETSYRGFYRAYQAHISSSNWAEFENASRNWHI
3D structure
PDB2bmo Structural insight into the dioxygenation of nitroarene compounds: the crystal structure of nitrobenzene dioxygenase.
ChainA
Resolution1.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2bmo, PDBe:2bmo, PDBj:2bmo
PDBsum2bmo
PubMed15854650
UniProtQ8RTL4

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