Structure of PDB 1i7q Chain C

Receptor sequence
>1i7qC (length=517) Species: 615 (Serratia marcescens) [Search protein sequence]
TKPQLTLLKVQASYRGDPTTLFHQLCGARPATLLLESAEINDKQNLQSLL
VIDSALRITALGHTVSVQALTANGPALLPLLDEALPPEVRNQARPNGREL
TFPAIDAVQDEDARLRSLSVFDALRTILTLVDSPADEREAVMLGGLFAYD
LVAGFENLPALRQDQRCPDFCFYLAETLLVLDHQRGSARLQASVFSEQAS
EAQRLQHRLEQLQAELQQPPQPIPHQKLENMQLSCNQSDEEYGAVVSELQ
EAIRQGEIFQVVPSRRFSLPCPAPLGPYQTLKDNNPSPYMFFMQDDDFTL
FGASPESALKYDAGNRQIEIYPIAGTRPRGRRADGSLDLDLDSRIELEMR
TDHKELAEHLMLVDLARNDLARICQAGSRYVADLTKVDRYSFVMHLVSRV
VGTLRADLDVLHAYQACMNMGTLSGAPKVRAMQLIAALRSTRRGSYGGRV
GYFTAVRNLDTCIVIRSAYVEDGHRTVQAGAGVVQDSIPEREADETRNKA
RAVLRAIATAHHAKEVF
3D structure
PDB1i7q The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan.
ChainC
Resolution1.95 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) Q260 E306 A324 E358 H395 T422 Y446 R466 G482 E495 K499
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 MG C E361 E498 E358 E495
BS02 PYR C Y449 I468 R469 A482 G483 K502 Y446 I465 R466 A479 G480 K499
Gene Ontology
Molecular Function
GO:0004049 anthranilate synthase activity
GO:0005515 protein binding
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:1i7q, PDBe:1i7q, PDBj:1i7q
PDBsum1i7q
PubMed11371633
UniProtP00897|TRPE_SERMA Anthranilate synthase component 1 (Gene Name=trpE)

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