Structure of PDB 1i1q Chain A

Receptor sequence
>1i1qA (length=512) [Search protein sequence]
KPTLELLTCDAAYRENPTALFHQVCGDRPATLLLESADIDSKDDLKSLLL
VDSALRITALGDTVTIQALSDNGASLLPLLDTALPAGVENDVLPAGRVLR
FPPVSPLLDENARLCSLSVFDAFRLLQGVVNIPTQEREAMFFGGLFAYDL
VAGFEALPHLEAGNNCPDYCFYLAETLMVIDHQKKSTRIQASLFTASDRE
KQRLNARLAYLSQQLTQPAPPLPVTPVPDMRCECNQSDDAFGAVVRQLQK
AIRAGEIFQVVPSRRFSLPCPSPLAAYYVLKKSNPSPYMFFMQDNDFTLF
GASPESSLKYDAASRQIEIYPIAGTRPRGRRADGTLDRDLDSRIELDMRT
DHKELSEHLMLVDLARNDLARICTPGSRYVADLTKVDRYSYVMHLVSRVV
GELRHDLDALHAYRACMNMGTLSGAPKVRAMQLIADAEGQRRGSYGGAVG
YFTAHGDLDTCIVIRSALVENGIATVQAGAGIVLDSVPQSEADETRNKAR
AVLRAIATAHHA
3D structure
PDB1i1q Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q263 E309 A327 E361 H398 T425 Y449 R469 G485 E498 K502
Catalytic site (residue number reindexed from 1) Q259 E305 A323 E357 H394 T421 Y445 R465 G481 E494 K498
Enzyme Commision number 4.1.3.27: anthranilate 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 TRP A L38 E39 S40 K50 P291 Y292 M293 G454 C465 L34 E35 S36 K46 P287 Y288 M289 G450 C461
Gene Ontology
Molecular Function
GO:0004049 anthranilate synthase activity
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0009058 biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1i1q, PDBe:1i1q, PDBj:1i1q
PDBsum1i1q
PubMed11224570
UniProtP00898|TRPE_SALTY Anthranilate synthase component 1 (Gene Name=trpE)

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