Structure of PDB 3uwz Chain B

Receptor sequence
>3uwzB (length=250) Species: 282458 (Staphylococcus aureus subsp. aureus MRSA252) [Search protein sequence]
MRTPIIAGNWKMNKTVQEAKDFVNALPTLPDSKEVESVICAPAIQLDALT
TAVKEGKAQGLEIGAQNTYFEDNGAFTGETSPVALADLGVKYVVIGHSER
RELFHETDEEINKKAHAIFKHGMTPIICVGETDEERESGKANDVVGEQVK
KAVAGLSEDQLKSVVIAYEPIWAIKSSTSEDANEMCAFVRQTIADLSSKE
VSEATRIQYGGSVKPNNIKEYMAQTDIDGALVGGASLKVEDFVQLLEGAK
3D structure
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
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 PO4 B M225 Q227 I230 M222 Q224 I227
BS02 G2H B K11 S215 G236 G237 K11 S212 G233 G234
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

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Cellular Component
External links
PDB RCSB:3uwz, PDBe:3uwz, PDBj:3uwz
PDBsum3uwz
PubMed22813930
UniProtQ6GIL6|TPIS_STAAR Triosephosphate isomerase (Gene Name=tpiA)

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