Structure of PDB 4csm Chain A

Receptor sequence
>4csmA (length=252) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MDFTKPETVLNLQNIRDELVRMEDSIIFKFIERSHFATCPSVYEANHPGL
EIPNFKGSFLDWALSNLEIAHSRIRRFESPDETPFFPDKIQKSFLPSINY
PQILAPYAPEVNYNDKIKKVYIEKIIPLISKRDGDDKNNFGSVATRDIEC
LQSLSRRIHFGKFVAEAKFQSDIPLYTKLIKSKDVEGIMKNITNSAVEEK
ILERLTKKAEVYGVDPTERRITPEYLVKIYKEIVIPITKEVEVEYLLRRL
EE
3D structure
PDB4csm Mechanisms of catalysis and allosteric regulation of yeast chorismate mutase from crystal structures.
ChainA
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) R16 R157 K168 N194 E198 T242 E246
Catalytic site (residue number reindexed from 1) R16 R157 K168 N194 E198 T238 E242
Enzyme Commision number 5.4.99.5: chorismate mutase.
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 TSA A R16 R157 K168 T193 N194 E198 I239 K243 E246 R16 R157 K168 T193 N194 E198 I235 K239 E242
Gene Ontology
Molecular Function
GO:0004106 chorismate mutase activity
GO:0005515 protein binding
GO:0016853 isomerase activity
GO:0072545 L-tyrosine binding
GO:0120284 tryptophan binding
Biological Process
GO:0006571 tyrosine biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0009094 L-phenylalanine biosynthetic process
GO:0046417 chorismate metabolic process
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4csm, PDBe:4csm, PDBj:4csm
PDBsum4csm
PubMed9384560
UniProtP32178|CHMU_YEAST Chorismate mutase (Gene Name=ARO7)

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