Structure of PDB 3ypi Chain B

Receptor sequence
>3ypiB (length=247) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
ARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSV
SLVKKPQVTVGAQNAYLKASGAFTGENSVDQIKDVGAKWVILGQSERRSY
FHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVL
EEVKDWTNVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAA
SELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPEFVDIINSRN
3D structure
PDB3ypi Electrophilic catalysis in triosephosphate isomerase: the role of histidine-95.
ChainB
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N10 K12 Q95 E97 E165 G171 S211
Catalytic site (residue number reindexed from 1) N9 K11 Q94 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 PGH B E165 I170 G171 G210 S211 L230 G232 E164 I169 G170 G209 S210 L229 G231
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

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Cellular Component
External links
PDB RCSB:3ypi, PDBe:3ypi, PDBj:3ypi
PDBsum3ypi
PubMed2007138
UniProtP00942|TPIS_YEAST Triosephosphate isomerase (Gene Name=TPI1)

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