Structure of PDB 1t0s Chain A Binding Site BS02

Receptor Information
>1t0s Chain A (length=491) Species: 316 (Stutzerimonas stutzeri) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SMLKREDWYDLTRTTNWTPKYVTENELFPEEMSGARGISMEAWEKYDEPY
KITYPEYVSIQREKDSGAYSIKAALERDGFVDRADPGWVSTMQLHFGAIA
LEEYAASTAEARMARFAKAPGNRNMATFGMMDENRHGQIQLYFPYANVKR
SRKWDWAHKAIHTNEWAAIAARSFFDDMMMTRDSVAVSIMLTFAFETGFT
NMQFLGLAADAAEAGDHTFASLISSIQTDESRHAQQGGPSLKILVENGKK
DEAQQMVDVAIWRSWKLFSVLTGPIMDYYTPLESRNQSFKEFMLEWIVAQ
FERQLLDLGLDKPWYWDQFMQDLDETHHGMHLGVWYWRPTVWWDPAAGVS
PEEREWLEEKYPGWNDTWGQCWDVITDNLVNGKPELTVPETLPTICNMCN
LPIAHTPGNKWNVKDYQLEYEGRLYHFGSEADRWCFQIDPERYKNHTNLV
DRFLKGEIQPADLAGALMYMSLEPGVMGDDAHDYEWVKAYQ
Ligand information
Ligand IDFE
InChIInChI=1S/Fe/q+3
InChIKeyVTLYFUHAOXGGBS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Fe+3]
FormulaFe
NameFE (III) ION
ChEMBL
DrugBankDB13949
ZINC
PDB chain1t0s Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1t0s Crystal Structure of the Toluene/o-Xylene Monooxygenase Hydroxylase from Pseudomonas stutzeri OX1: INSIGHT INTO THE SUBSTRATE SPECIFICITY, SUBSTRATE CHANNELING, AND ACTIVE SITE TUNING OF MULTICOMPONENT MONOOXYGENASES.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		E104 E134 H137
Binding residue
(residue number reindexed from 1)		E103 E133 H136
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E104 E134 H137 E197 E231 H234
Catalytic site (residue number reindexed from 1) E103 E133 H136 E196 E230 H233
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding

View graph for
Molecular Function
External links
PDB RCSB:1t0s, PDBe:1t0s, PDBj:1t0s
PDBsum1t0s
PubMed15096510
UniProtO87798

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