Structure of PDB 3tao Chain A

Receptor sequence
>3taoA (length=256) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
SRKPLIAGNWKMNLNHYEAIALVQKIAFSLPDKYYDRVDVAVIPPFTDLR
SVQTLVDGDKLRLTYGAQDLSPHDSGAYTGDVSGAFLAKLGCSYVVVGHS
ERRTYHNEDDALVAAKAATALKHGLTPIVCIGEHLDVREAGNHVAHNIEQ
LRGSLAGLLAEQIGSVVIAYEPVWAIGTGRVASAADAQEVCAAIRKELAS
LASPRIADTVRVLYGGSVNAKNVGDIVAQDDVDGGLVGGASLDGEHFATL
AAIAAG
3D structure
PDB3tao Structural and functional characterization of Mycobacterium tuberculosis triosephosphate isomerase.
ChainA
Resolution1.45 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 H100 E102 E172 G178 S218
Catalytic site (residue number reindexed from 1) N9 K11 H99 E101 E171 G177 S217
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 A K12 H100 I177 G178 G217 S218 L237 G239 G240 K11 H99 I176 G177 G216 S217 L236 G238 G239 MOAD: Kd=7.28uM
PDBbind-CN: -logKd/Ki=5.14,Kd=7.28uM
BS02 PGH A R51 S52 T55 R50 S51 T54 MOAD: Kd=7.28uM
PDBbind-CN: -logKd/Ki=5.14,Kd=7.28uM
Gene Ontology
Molecular Function
GO:0004807 triose-phosphate isomerase activity
GO:0005515 protein binding
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:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3tao, PDBe:3tao, PDBj:3tao
PDBsum3tao
PubMed22120738
UniProtP9WG43|TPIS_MYCTU Triosephosphate isomerase (Gene Name=tpiA)

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