Structure of PDB 1et0 Chain A Binding Site BS01

Receptor Information
>1et0 Chain A (length=254) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFLINGHKQESLAVSDRATQFGDGCFTTARVIDGKVSLLSAHIQRLQDAC
QRLMISCDFWPQLEQEMKTLAAEQQNGVLKVVISRGSGGRGYSTLNSGPA
TRILSVTAITLALSPVRLGRNPHLAGIKHLNRLEQVLIRSHLEQTNADEA
LVLDSEGWVTECCAANLFWRKGNVVYTPRLDQAGVNGIMRQFCIRLLAQS
SYQLVEVQASLEESLQADEMVICNALMPVMPVCACGDVSFSSATLYEYLA
PLCE
Ligand information
Ligand IDPLP
InChIInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain1et0 Chain A Residue 413 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1et0 Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		R59 K159 E193 A196 A197 V217 G219 I220 M221 N256 A257
Binding residue
(residue number reindexed from 1)		R45 K128 E161 A164 A165 V185 G187 I188 M189 N224 A225
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) F36 T38 I158 K159 E193 V217
Catalytic site (residue number reindexed from 1) F26 T28 I127 K128 E161 V185
Enzyme Commision number 4.1.3.38: aminodeoxychorismate lyase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008696 4-amino-4-deoxychorismate lyase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
Biological Process
GO:0008153 para-aminobenzoic acid biosynthetic process
GO:0046394 carboxylic acid biosynthetic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1et0, PDBe:1et0, PDBj:1et0
PDBsum1et0
PubMed10876155
UniProtP28305|PABC_ECOLI Aminodeoxychorismate lyase (Gene Name=pabC)

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