Structure of PDB 1pii Chain A

Receptor sequence

>1piiA (length=452) Species: 562 (Escherichia coli)

MQTVLAKIVADKAIWVEARKQQQPLASFQNEVQPSTRHFYDALQGARTAF
ILECKKASPSKGVIRDDFDPARIAAIYKHYASAISVLTDEKYFQGSFNFL
PIVSQIAPQPILCKDFIIDPYQIYLARYYQADACLLMLSVLDDDQYRQLA
AVAHSLEMGVLTEVSNEEEQERAIALGAKVVGINNRDLRDLSIDLNRTRE
LAPKLGHNVTVISESGINTYAQVRELSHFANGFLIGSALMAHDDLHAAVR
RVLLGENKVCGLTRGQDAKAAYDAGAIYGGLIFVATSPRCVNVEQAQEVM
AAAPLQYVGVFRNHDIADVVDKAKVLSLAAVQLHGNEEQLYIDTLREALP
AHVAIWKALSVGETLPAREFQHVDKYVLDNGQGGSGQRFDWSLLNGQSLG
NVLLAGGLGADNCVEAAQTGCAGLDFNSAVESQPGIKDARLLASVFQTLR
AY

3D structure

• PDB: 1pii Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution.
• Chain: A
• Resolution: 2.0 Å

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.

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	PO4	A	K55 S215 I235 G236 S237	K55 S215 I235 G236 S237
BS02	PO4	A	G386 G407 N427 S428	G386 G407 N427 S428

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

External links

• PDB: RCSB:1pii, PDBe:1pii, PDBj:1pii
• PDBsum: 1pii
• PubMed: 1738159
• UniProt: P00909|TRPC_ECOLI Tryptophan biosynthesis protein TrpCF (Gene Name=trpC)