Structure of PDB 1w85 Chain C Binding Site BS02

Receptor Information
>1w85 Chain C (length=365) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TFQFPFAEQLEKVAEQFPTFQILNEEGEVVNEEAMPELSDEQLKELMRRM
VYTRILDQRSISLNRQGRLGFYAPTAGQEASQIASHFALEKEDFILPGYR
DVPQIIWHGLPLYQAFLFSRGHFHGNQIPEGVNVLPPQIIIGAQYIQAAG
VALGLKMRGKKAVAITYTGDGGTSQGDFYEGINFAGAFKAPAIFVVQNNR
FAISTPVEKQTVAKTLAQKAVAAGIPGIQVDGMDPLAVYAAVKAARERAI
NGEGPTLIETLCFRYGPHTMSGDDPTRYRSKELENEWAKKDPLVRFRKFL
EAKGLWSEEEENNVIEQAKEEIKEAIKKADETPKQKVTDLISIMFEELPF
NLKEQYEIYKEKESK
Ligand information
Ligand IDTPP
InChIInChI=1S/C12H18N4O7P2S/c1-8-11(3-4-22-25(20,21)23-24(17,18)19)26-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H4-,13,14,15,17,18,19,20,21)/p+1
InChIKeyAYEKOFBPNLCAJY-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P@@](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCO[P@](=O)(O)OP(=O)(O)O
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)OP(=O)(O)O
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P](O)(=O)O[P](O)(O)=O)c2C)c(N)n1
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCCc1sc[n+](c1C)Cc2c(nc(nc2)C)N
FormulaC12 H19 N4 O7 P2 S
NameTHIAMINE DIPHOSPHATE
ChEMBLCHEMBL1236376
DrugBank
ZINCZINC000008215517
PDB chain1w85 Chain C Residue 1370 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1w85 A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		Y102 R103 I142 I144 G172 D173 G174 G175 N202 A205 I206 H271
Binding residue
(residue number reindexed from 1)		Y99 R100 I139 I141 G169 D170 G171 G172 N199 A202 I203 H268
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) S65 I142 R267 H271 T272 Y281
Catalytic site (residue number reindexed from 1) S62 I139 R264 H268 T269 Y278
Enzyme Commision number 1.2.4.1: pyruvate dehydrogenase (acetyl-transferring).
Gene Ontology
Molecular Function
GO:0004739 pyruvate dehydrogenase (acetyl-transferring) activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0016624 oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor
Biological Process
GO:0009083 branched-chain amino acid catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1w85, PDBe:1w85, PDBj:1w85
PDBsum1w85
PubMed15514159
UniProtP21873|ODPA_GEOSE Pyruvate dehydrogenase E1 component subunit alpha (Gene Name=pdhA)

[Back to BioLiP]