Structure of PDB 1ssg Chain B

Receptor sequence

>1ssgB (length=247) Species: 9031 (Gallus gallus)

APRKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFA
RQKLDAKIGVAAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHSERRHV
FGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKAIA
DNVKDWSKVVLAYEPVWAIGTGYSLTPQQAQEVHEKLRGWLKSHVSDAVA
QSTRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDIINAKH

3D structure

• PDB: 1ssg Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase
• Chain: B
• Resolution: 2.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N11 K13 H95 E97 E165 G171 S211
• Catalytic site (residue number reindexed from 1): N10 K12 H94 E96 E164 G170 S210
• Enzyme Commision number: 4.2.3.3: methylglyoxal synthase.
  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	PGA	B	K13 H95 E165 I170 G171 S211 G232 G233	K12 H94 E164 I169 G170 S210 G231 G232

Gene Ontology

Molecular Function

• GO:0004807 triose-phosphate isomerase activity
• GO:0008929 methylglyoxal synthase activity
• GO:0016829 lyase activity
• GO:0016853 isomerase activity
• GO:0031625 ubiquitin protein ligase binding
• GO:0042803 protein homodimerization activity

Biological Process

• GO:0006006 glucose metabolic process
• GO:0006094 gluconeogenesis
• GO:0006096 glycolytic process
• GO:0019242 methylglyoxal biosynthetic process
• GO:0019563 glycerol catabolic process
• GO:0019682 glyceraldehyde-3-phosphate metabolic process
• GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
• GO:0061621 canonical glycolysis

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1ssg, PDBe:1ssg, PDBj:1ssg
• PDBsum: 1ssg
• PubMed: 15166315
• UniProt: P00940|TPIS_CHICK Triosephosphate isomerase (Gene Name=TPI1)