Structure of PDB 2jgq Chain B

Receptor sequence
>2jgqB (length=231) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
TKIAMANFKSAMPIFKSHAYLKELEKTLKPQHFDRVFVFPDFFGLLPNSF
LHFTLGVQNAYPRDCGAFTGEITSKHLEELKIHTLLIGHSERRTLLKESP
SFLKEKFDFFKSKNFKIVYCIGEELTTREKGFKAVKEFLSEQLENIDLNY
PNLVVAYEPIWAIGTSASLEDIYLTHGFLKQILNQKTPLLYGGSVNTQNA
KEILGIDSVDGLLIGSASWELENFKTIISFL
3D structure
PDB2jgq Kinetics and Structural Properties of Triosephosphate Isomerase from Helicobacter Pylori
ChainB
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N8 K10 H90 E92 E159 G165 S197
Catalytic site (residue number reindexed from 1) N7 K9 H89 E91 E158 G164 S194
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 K10 I164 G165 S197 G218 S219 K9 I163 G164 S194 G215 S216
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:2jgq, PDBe:2jgq, PDBj:2jgq
PDBsum2jgq
PubMed17957775
UniProtP56076|TPIS_HELPY Triosephosphate isomerase (Gene Name=tpiA)

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