Structure of PDB 1ml1 Chain C

Receptor sequence
>1ml1C (length=241) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVASTFVHLAMTK
ERLSHPKFVIAAQNAGNADALASLKDFGVNWIVLGHSERRWYYGETNEIV
ADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADW
AKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRIL
YGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ
3D structure
PDB1ml1 Protein engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop.
ChainC
Resolution2.6 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 H95 E97 E167 G173 S213
Catalytic site (residue number reindexed from 1) N10 K12 H86 E88 E158 G164 S204
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 C N11 K13 H95 E167 I172 G173 S213 G234 G235 N10 K12 H86 E158 I163 G164 S204 G225 G226
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
GO:0020015 glycosome

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Cellular Component
External links
PDB RCSB:1ml1, PDBe:1ml1, PDBj:1ml1
PDBsum1ml1
PubMed9089815
UniProtP04789|TPIS_TRYBB Triosephosphate isomerase, glycosomal

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