Structure of PDB 2ypi Chain B

Receptor sequence

>2ypiB (length=247) Species: 4932 (Saccharomyces cerevisiae)

ARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSV
SLVKKPQVTVGAQNAYLKASGAFTGENSVDQIKDVGAKWVILGHSERRSY
FHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVL
EEVKDWTNVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAA
SELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFVDIINSRN

3D structure

• PDB: 2ypi Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
• Chain: B
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): N10 K12 H95 E97 E165 G171 S211
• Catalytic site (residue number reindexed from 1): N9 K11 H94 E96 E164 G170 S210
• 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	PGA	B	K12 H95 E165 A169 I170 G171 G210 S211 L230 G232	K11 H94 E164 A168 I169 G170 G209 S210 L229 G231	MOAD: Ki=15uM PDBbind-CN: -logKd/Ki=4.82,Ki=15uM

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:0005739 mitochondrion
• GO:0005829 cytosol
• GO:0005886 plasma membrane

External links

• PDB: RCSB:2ypi, PDBe:2ypi, PDBj:2ypi
• PDBsum: 2ypi
• PubMed: 2204418
• UniProt: P00942|TPIS_YEAST Triosephosphate isomerase (Gene Name=TPI1)