Structure of PDB 1i7s Chain C

Receptor sequence
>1i7sC (length=511) Species: 615 (Serratia marcescens) [Search protein sequence]
TKPQLTLLKVQASYRGDPTTLFHQLCGARPATLLLESAELQSLLVIDSAL
RITALGHTVSVQALTANGPALLPLLDEALPPEVRNQARPNGRELTFPAID
AVQDEDARLRSLSVFDALRTILTLVDSPADEREAVMLGGLFAYDLVAGFE
NLPALRQDQRCPDFCFYLAETLLVLDHQRGSARLQASVFSEQASEAQRLQ
HRLEQLQAELQQPPQPIPHQKLENMQLSCNQSDEEYGAVVSELQEAIRQG
EIFQVVPSRRFSLPCPAPLGPYQTLKDNNPSPYMFFMQDDDFTLFGASPE
SALKYDAGNRQIEIYPIAGTRPRGRRADGSLDLDLDSRIELEMRTDHKEL
AEHLMLVDLARNDLARICQAGSRYVADLTKVDRYSFVMHLVSRVVGTLRA
DLDVLHAYQACMNMGTLSGAPKVRAMQLIAALRSTRRGSYGGRVGYFTAV
RNLDTCIVIRSAYVEDGHRTVQAGAGVVQDSIPEREADETRNKARAVLRA
IATAHHAKEVF
3D structure
PDB1i7s 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
Resolution2.4 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) Q254 E300 A318 E352 H389 T416 Y440 R460 G476 E489 K493
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 C L38 E39 S40 L49 Q50 P291 Y292 M293 G454 C465 L35 E36 S37 L40 Q41 P282 Y283 M284 G445 C456
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:1i7s, PDBe:1i7s, PDBj:1i7s
PDBsum1i7s
PubMed11371633
UniProtP00897|TRPE_SERMA Anthranilate synthase component 1 (Gene Name=trpE)

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