Structure of PDB 5xbp Chain A

Receptor sequence
>5xbpA (length=444) Species: 1302548 (Diaphorobacter sp. DS2) [Search protein sequence]
SYQNLVSEAGLTQKHLIHGDKELFQHEMKTIFARNWLFLTHDSLIPSPGD
YVTAKMGLDEVIVSRQNDGSVRAFLNVCRHRGKTIVHAEAGNAKGFVCNY
HGWGYGTNGELQSVPFEKELYGDAIKKKCLGLKEVPRIESFHGFIYGCFD
AEAPPLIDYLGDAAWYMEPTFKHSGGLELVGPPGKVVVKANWKTFAENFV
GDIYHVGWTHASILRVGQSVFTPLAGNAMLPPEGSGLQMTSKYGSGMSLM
WDYYAGNHSADLVPDLMAFGGAKQEKLAKEIGDVRARIYRSHLNGTIFPN
NSFLTGSAAFKVWNPIDENTTEVWTYAFVEKDMPEDLKRRLADAVQRTVG
PGGYWESDDNDNMETLSQNAKKYQSSNSDLIASLGFGKDVYGDECYPGVV
GPSGASETSYRGFYRAYQAHISSSNWAEFENASRNWHTELTKTT
3D structure
PDB5xbp Structural and functional studies of ferredoxin and oxygenase components of 3-nitrotoluene dioxygenase from Diaphorobacter sp. strain DS2.
ChainA
Resolution2.9 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) H101 D202 H205 H210 D359
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 FE A H206 H211 D360 H205 H210 D359
BS02 FES A C79 H81 R82 C99 Y101 H102 C78 H80 R81 C98 Y100 H101
Gene Ontology
Molecular Function
GO:0005506 iron ion 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:5xbp, PDBe:5xbp, PDBj:5xbp
PDBsum5xbp
PubMed28448625
UniProtM9PW10

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