Structure of PDB 3r75 Chain B

Receptor sequence
>3r75B (length=622) [Search protein sequence]
RNLFDRVLHGQAPCFALIARSTGSAGERAMIDVFAGAVSYPSSLAELPLA
APTATGADRQELLVMVPYRQLHERGFKTHDDGAPLVAITCDEHETVSAQL
ALAAIPDADTALGERHFDIDDEAYAEIVERVITDEIGTGAGSNFVIKRTL
EGDLDDYSPAKALAVFKRLMRREVGAYWIFVIHTGERTFVGATPERHLTL
HEGCATMNPISGTYRYPQSGPTIDGINAFLGDRKESDELYMVLDEELKMM
ARICPAGGQVTGPHLREMARLAHTEYFIVGHTEADVRDLLRETMFAPTVT
GSPIESATRVIARHERAGRGYYSGIAALIGRDARGGRTLDSAILIRTAEI
DRAGHVRIGVGSTLVRHSDAVSEVMETHAKVAALSNAFDPPEAGPALGQH
PSVQAALRERNEGIADFWFRPYGGRAELSGCRALIVDAEDHFTAMIAQQL
SSLGLATEVCGVHDAVDLARYDVVVMGPGPGDPSDAGDPRIARLYAWLRH
LIDEGKPFMAVCLSHQILNAILGIPLVRREVPNQGIQVEIDLFGQRERVG
FYNTYVAQTVRDEMDVDGVGTVAISRDPRTGEVHALRGPTFSSMQFHAES
VLTVDGPRILGEAITHAIRREK
3D structure
PDB3r75 Ligand Binding Induces an Ammonia Channel in 2-Amino-2-desoxyisochorismate (ADIC) Synthase PhzE.
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N149 E201 E244 H279 T304 Y328 R352 T369 E382 K386
Catalytic site (residue number reindexed from 1) N143 E195 E238 H273 T298 Y322 R346 T363 E376 K380
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 B E244 E382 E238 E376
BS02 PYR B Y328 R352 V366 G367 K386 Y322 R346 V360 G361 K380
BS03 ZN B C526 Y566 H611 C512 Y552 H597
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:0006541 glutamine metabolic process
GO:0009058 biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:3r75, PDBe:3r75, PDBj:3r75
PDBsum3r75
PubMed21454481
UniProtQ396C7

[Back to BioLiP]