Structure of PDB 5hud Chain D

Receptor sequence
>5hudD (length=457) Species: 1718 (Corynebacterium glutamicum) [Search protein sequence]
HHSSGMSWTVDILPEGMQQQFEDTISRDAKQQPTWDRAQAENVRKILESV
PPIVVAPEVLELKQKLADVANGKAFLLQGGDCAETFESNTEPHIRANVKT
LLQMAVVLTYGASTPVIKMARIAGQYAKPRSSDLDGNGLPNYRGDIVNGV
EATPEARRHDPARMIRAYANASAAMNLVRALTSSGTADLYRLSEWNREFV
ANSPAGARYEALAREIDSGLRFMEACGVSDESLRAADIYCSHEALLVDYE
RSMLRLATDEEGNEELYDLSAHQLWIGERTRGMDDFHVNFASMISNPIGI
KIGPGITPEEAVAYADKLDPNFEPGRLTIVARMGHDKVRSVLPGVIQAVE
ASGHKVIWQSDPMHGNTFTASNGYKTRHFDKVIDEVQGFFEVHRALGTHP
GGIHIEFTGEDVTECLGGAEDITDVDLPGRYESACDPRLNTQQSLELAFL
VAEMLRN
3D structure
PDB5hud Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp.
ChainD
Resolution2.15 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 D C97 H379 E421 D451 C82 H364 E406 D436
BS02 TRP D A120 K133 A250 A105 K118 A235
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

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