Structure of PDB 4bi6 Chain A

Receptor sequence
>4bi6A (length=255) Species: 5741 (Giardia intestinalis) [Search protein sequence]
PARRPFIGGNFKCNGSLDFIKSHVAAIAAHKIPDSVDVVIAPSAVHLSTA
IAANTSKQLRIAAQNVYLEGNGAWTGETSVEMLQDMGLKHVIVGHSERRR
IMGETDEQSAKKAKRALEKGMTVIFCVGETLDERKANRTMEVNIAQLEAL
GKELGESKMLWKEVVIAYEPVWSIGTGVVATPEQAEEVHVGLRKWFVEKV
AAEGAQHIRIIYGGSANGSNNEKLGQCPNIDGFLVGGASLKPEFMTMIDI
LTKTR
3D structure
PDB4bi6 Structural and Functional Perturbation of Giardia Lamblia Triosephosphate Isomerase by Modification of a Non-Catalytic, Non-Conserved Region.
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) N11 K13 H96 E98 E170 G176 S216
Catalytic site (residue number reindexed from 1) N10 K12 H95 E97 E169 G175 S215
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 A K13 H96 E170 I175 G176 G215 S216 L235 G237 G238 K12 H95 E169 I174 G175 G214 S215 L234 G236 G237 MOAD: Kd=113.3uM
PDBbind-CN: -logKd/Ki=3.95,Kd=113.3uM
Gene Ontology
Molecular Function
GO:0004807 triose-phosphate isomerase activity
GO:0008929 methylglyoxal synthase activity
GO:0016829 lyase 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:4bi6, PDBe:4bi6, PDBj:4bi6
PDBsum4bi6
PubMed23894402
UniProtP36186|TPI1_GIAIN Triosephosphate isomerase

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