Structure of PDB 3uwu Chain A

Receptor sequence

>3uwuA (length=253) Species: 282458 (Staphylococcus aureus subsp. aureus MRSA252)

MRTPIIAGNWKMNKTVQEAKDFVNALPTLPDSKEVESVICAPAIQLDALT
TAVKEGKAQGLEIGAQNTYFEDNGAFTGETSPVALADLGVKYVVIGHSER
RELFHETDEEINKKAHAIFKHGMTPIICVGETDEERESGKANDVVGEQVK
KAVAGLSEDQLKSVVIAYEPIWAIGTGKSSTSEDANEMCAFVRQTIADLS
SKEVSEATRIQYGGSVKPNNIKEYMAQTDIDGALVGGASLKVEDFVQLLE
GAK

3D structure

• PDB: 3uwu 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
• Chain: A
• Resolution: 2.15 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N9 K11 H97 E99 E169 G175 S215
• Catalytic site (residue number reindexed from 1): N9 K11 H97 E99 E169 G175 S215
• 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	G3P	A	N9 K11 H97 E169 I174 G175 S215 L234 G236 G237	N9 K11 H97 E169 I174 G175 S215 L234 G236 G237

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

External links

• PDB: RCSB:3uwu, PDBe:3uwu, PDBj:3uwu
• PDBsum: 3uwu
• PubMed: 22813930
• UniProt: Q6GIL6|TPIS_STAAR Triosephosphate isomerase (Gene Name=tpiA)