Structure of PDB 1pii Chain A Binding Site BS01

Receptor Information
>1pii Chain A (length=452) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MQTVLAKIVADKAIWVEARKQQQPLASFQNEVQPSTRHFYDALQGARTAF
ILECKKASPSKGVIRDDFDPARIAAIYKHYASAISVLTDEKYFQGSFNFL
PIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDDQYRQLA
AVAHSLEMGVLTEVSNEEEQERAIALGAKVVGINNRDLRDLSIDLNRTRE
LAPKLGHNVTVISESGINTYAQVRELSHFANGFLIGSALMAHDDLHAAVR
RVLLGENKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVM
AAAPLQYVGVFRNHDIADVVDKAKVLSLAAVQLHGNEEQLYIDTLREALP
AHVAIWKALSVGETLPAREFQHVDKYVLDNGQGGSGQRFDWSLLNGQSLG
NVLLAGGLGADNCVEAAQTGCAGLDFNSAVESQPGIKDARLLASVFQTLR
AY
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain1pii Chain A Residue 453 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1pii Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		K55 S215 I235 G236 S237
Binding residue
(residue number reindexed from 1)		K55 S215 I235 G236 S237
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E53 K55 K114 E163 N184 E214 S215 C260 D379
Catalytic site (residue number reindexed from 1) E53 K55 K114 E163 N184 E214 S215 C260 D379
Enzyme Commision number 4.1.1.48: indole-3-glycerol-phosphate synthase.
5.3.1.24: phosphoribosylanthranilate isomerase.
Gene Ontology
Molecular Function
GO:0004425 indole-3-glycerol-phosphate synthase activity
GO:0004640 phosphoribosylanthranilate isomerase activity
GO:0016830 carbon-carbon lyase activity
GO:0016831 carboxy-lyase activity
GO:0016853 isomerase activity
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0006568 tryptophan metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1pii, PDBe:1pii, PDBj:1pii
PDBsum1pii
PubMed1738159
UniProtP00909|TRPC_ECOLI Tryptophan biosynthesis protein TrpCF (Gene Name=trpC)

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