Structure of PDB 5hud Chain A

Receptor sequence
>5hudA (length=444) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
PEGMQQQFEDTISRDAKQQPTWDRAQAENVRKILESVPPIVVAPEVLELK
QKLADVANGKAFLLQGGDCAETFESNTEPHIRANVKTLLQMAVVLTYGAS
TPVIKMARIAGQYAKPRSSDLDGNGLPNYRGDIVNGVEATPEARRHDPAR
MIRAYANASAAMNLVRALTSSGTADLYRLSEWNREFVANSPAGARYEALA
REIDSGLRFMEACGVSDESLRAADIYCSHEALLVDYERSMLRLATDEEGN
EELYDLSAHQLWIGERTRGMDDFHVNFASMISNPIGIKIGPGITPEEAVA
YADKLDPNFEPGRLTIVARMGHDKVRSVLPGVIQAVEASGHKVIWQSDPM
HGNTFTASNGYKTRHFDKVIDEVQGFFEVHRALGTHPGGIHIEFTGEDVT
ECLGGAEDITDVDLPGRYESACDPRLNTQQSLELAFLVAEMLRN
3D structure
PDB5hud Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp.
ChainA
Resolution2.15 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 C69 H351 E393 D423
BS02 TRP A A120 V121 K133 A202 S247 A250 A92 V93 K105 A174 S219 A222
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5hud, PDBe:5hud, PDBj:5hud
PDBsum5hud
PubMed29178787
UniProtQ8NNL5

[Back to BioLiP]