Structure of PDB 4p53 Chain A

Receptor sequence
>4p53A (length=360) Species: 1133850 (Streptomyces hygroscopicus subsp. jinggangensis 5008) [Search protein sequence]
WRVSALKEVSYDVVVQPRLLANPALADALSARRLIVIDATVRSLYGEQLA
AYLAGHDVEFHLCVIDAHESAKVMETVFEVVDAMDAFGVPRRHAPVLAMG
GGVLTDIVGLAASLYRRATPYVRIPTTLIGMIDAGIGAKTGVNFREHKNR
LGTYHPSSLTLIDPGFLATLDARHLRNGLAEILKVALVKDAELFDLLEGH
GASLVEQRMQPGAALTVLRRAVQGMLEELQPNLWEHQLRRLVDFGHSFSP
SVEMAALPELLHGEAVCIDMALSSVLAHHRGLLTEAELGRVLDVMRLLHL
PVLHPVCTPDLMRAALADTVKHRDGWQHMPLPRGIGDAVFVNDVTQREIE
AALLTLAERD
3D structure
PDB4p53 Structure of a sedoheptulose 7-phosphate cyclase: ValA from Streptomyces hygroscopicus.
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R149 K171 E213 M263 E273 R277 D281 H284 P288 H300
Catalytic site (residue number reindexed from 1) R117 K139 E181 M225 E235 R239 D243 H246 P250 H262
Enzyme Commision number 4.2.3.152: 2-epi-5-epi-valiolone 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 ZN A E213 H284 H300 E181 H246 H262
BS02 NAI A D70 T72 V73 L76 E101 K104 G133 G134 V135 D138 T158 T159 I161 D165 A166 K180 T201 L202 H206 H300 D38 T40 V41 L44 E69 K72 G101 G102 V103 D106 T126 T127 I129 D133 A134 K148 T169 L170 H174 H262
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003856 3-dehydroquinate synthase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0017000 antibiotic biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4p53, PDBe:4p53, PDBj:4p53
PDBsum4p53
PubMed24832673
UniProtH2K887|VALA_STRHJ 2-epi-5-epi-valiolone synthase (Gene Name=valA)

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