Structure of PDB 3uwz Chain B Binding Site BS01

Receptor Information
>3uwz Chain B (length=250) Species: 282458 (Staphylococcus aureus subsp. aureus MRSA252) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRTPIIAGNWKMNKTVQEAKDFVNALPTLPDSKEVESVICAPAIQLDALT
TAVKEGKAQGLEIGAQNTYFEDNGAFTGETSPVALADLGVKYVVIGHSER
RELFHETDEEINKKAHAIFKHGMTPIICVGETDEERESGKANDVVGEQVK
KAVAGLSEDQLKSVVIAYEPIWAIKSSTSEDANEMCAFVRQTIADLSSKE
VSEATRIQYGGSVKPNNIKEYMAQTDIDGALVGGASLKVEDFVQLLEGAK
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain3uwz Chain B Residue 255 [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]
PDB3uwz Crystal structures of triosephosphate isomerase from methicillin resistant Staphylococcus aureus MRSA252 provide structural insights into novel modes of ligand binding and unique conformations of catalytic loop
Resolution2.5 Å
Binding residue
(original residue number in PDB)		M225 Q227 I230
Binding residue
(residue number reindexed from 1)		M222 Q224 I227
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) N9 K11 H97 E99 E169 S215
Catalytic site (residue number reindexed from 1) N9 K11 H97 E99 E169 S212
Enzyme Commision number 5.3.1.1: triose-phosphate isomerase.
Gene Ontology
Molecular Function
GO:0004807 triose-phosphate isomerase activity
GO:0016853 isomerase activity
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0019563 glycerol catabolic process
GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3uwz, PDBe:3uwz, PDBj:3uwz
PDBsum3uwz
PubMed22813930
UniProtQ6GIL6|TPIS_STAAR Triosephosphate isomerase (Gene Name=tpiA)

[Back to BioLiP]