Structure of PDB 5huc Chain A

Receptor sequence
>5hucA (length=449) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
DLPPLPEGMQQQFEDTISRDAKQQPTWDRAQAENVRKILESVPPIVVAPE
VLELKQKLADVANGKAFLLQGGDCAETFESNTEPHIRANVKTLLQMAVVL
TYGASTPVIKMARIAGQYAKPRSSDLDGNGLPNYRGDIVNGVEATPEARR
HDPARMIRAYANASAAMNLVRALTSSGTADLYRLSEWNREFVANSPAGAR
YEALAREIDSGLRFMEACGVSDESLRAADIYCSHEALLVDYERSMLRLAT
DEEGNEELYDLSAHQLWIGERTRGMDDFHVNFASMISNPIGIKIGPGITP
EEAVAYADKLDPNFEPGRLTIVARMGHDKVRSVLPGVIQAVEASGHKVIW
QSDPMHGNTFTASNGYKTRHFDKVIDEVQGFFEVHRALGTHPGGIHIEFT
GEDVTECLGGAEDITDVDLPGRYESACDPRLNTQQSLELAFLVAEMLRN
3D structure
PDB5huc Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp.
ChainA
Resolution2.45 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 C74 H356 E398 D428
BS02 PEP A R136 E258 W290 G292 E293 K316 R347 H379 R113 E235 W267 G269 E270 K293 R324 H356
BS03 TRP A A120 V121 K133 S247 A97 V98 K110 S224
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
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Biological Process
External links
PDB RCSB:5huc, PDBe:5huc, PDBj:5huc
PDBsum5huc
PubMed29178787
UniProtQ8NNL5

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