Structure of PDB 7ten Chain Q

Receptor sequence
>7tenQ (length=442) Species: 1639 (Listeria monocytogenes) [Search protein sequence]
KYTKEDIFRFADEQNVKFIRLQFTDILGIIKNVEIPVSQLKKALDNKIMF
DGSSIEGFVRIEESDMYLFPDLDTWVVFPWTAEKGKVARMICDIYNPDMT
PFAGDPRANLKRVLKEMEELGFTEFNLGPEPEFFLFKLDENRRPTLELND
SGGYFDLAPTDLGENCRRDIVLELEEMGFEIEASHHEVAPGQHEIDFKYE
DAITACDSIQTFKLVVKTIARKHGLHATFMPKPLFGVNGSGMHFNMSLFN
EKGNAFFDESGELELSQTAYHFLAGMLKHARGYTAVTNPTINSFKRLVPG
YEAPCYIAWSGKNRSPLVRVPSSRGLSTRLELRSVDPSANPYLAMAVLLK
AGLSGIKDELTPPAPVDRNIYGMNEEEREATGIYDLPESLGHALIELEKN
EIIKDGLGEHIFEHFIEAKTIECDMFRTAVHPWEREQYLEIY
3D structure
PDB7ten Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
ChainQ
Resolution3.5 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.1.2: glutamine synthetase.
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 ADP Q E132 E184 F199 Y201 N247 R316 R321 L328 R331 E130 E182 F197 Y199 N245 R314 R319 L326 R329
BS02 P3S Q E132 E134 E189 E196 N240 G241 G243 H245 R298 E304 R316 E130 E132 E187 E194 N238 G239 G241 H243 R296 E302 R314
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006542 glutamine biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7ten, PDBe:7ten, PDBj:7ten
PDBsum7ten
PubMed35778410
UniProtA0A5D5GA79

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