Structure of PDB 5hue Chain A

Receptor sequence
>5hueA (length=447) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
PPLPEGMQQQFEDTISRDAKQQPTWDRAQAENVRKILESVPPIVVAPEVL
ELKQKLADVANGKAFLLQGGDCAETFESNTEPHIRANVKTLLQMAVVLTY
GASTPVIKMARIAGQYAKPRSSDLDGNGLPNYRGDIVNGVEATPEARRHD
PARMIRAYANASAAMNLVRALTSSGTADLYRLSEWNREFVANSPAGARYE
ALAREIDSGLRFMEACGVSDESLRAADIYCSHEALLVDYERSMLRLATDE
EGNEELYDLSAHQLWIGERTRGMDDFHVNFASMISNPIGIKIGPGITPEE
AVAYADKLDPNFEPGRLTIVARMGHDKVRSVLPGVIQAVEASGHKVIWQS
DPMHGNTFTASNGYKTRHFDKVIDEVQGFFEVHRALGTHPGGIHIEFTGE
DVTECLGGAEDITDVDLPGRYESACDPRLNTQQSLELAFLVAEMLRN
3D structure
PDB5hue Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp.
ChainA
Resolution2.65 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.54: 3-deoxy-7-phosphoheptulonate synthase.
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 MN A C97 H379 E421 D451 C72 H354 E396 D426
BS02 PEP A R136 E258 G292 E293 R294 K316 R347 H379 R111 E233 G267 E268 R269 K291 R322 H354
BS03 TRP A K133 S247 A250 K108 S222 A225
Gene Ontology
Molecular Function
GO:0003849 3-deoxy-7-phosphoheptulonate synthase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0008652 amino acid biosynthetic process
GO:0009073 aromatic amino acid family biosynthetic process
GO:0009423 chorismate biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5hue, PDBe:5hue, PDBj:5hue
PDBsum5hue
PubMed29178787
UniProtQ8NNL5

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