Structure of PDB 7tdp Chain C

Receptor sequence

>7tdpC (length=440) Species: 1406 (Paenibacillus polymyxa)

MSYTREDIIRIAEEENVRFIRLQFTDLLGTIKNVEIPVSQLEKALDNKMM
FDGSSIEGYVRIEESDMYLYPDLDTWVVFPWSDRVARLICDIYKPDGSPF
AGDPRGILKRVLKEAEELGYTSMNVGPEPEFFLFKTDEKGDPTTELNDQG
GYFDLAPMDLGENCRREIVLKLEEMGFEIEASHHEVAPGQHEIDFKYADA
VKAADQIQTFKLVVKTIARQHGLHATFMPKPLFGVNGSGMHCNQSLFKDN
ENVFYDETDELGLSQTARHYMAGILKHARAMAAITNPTVNSYKRLVPGYE
APCYVAWSASNRSPMIRIPASRGLSTRVEVRNPDPAANPYLALAVMLRAG
LDGIKRQMALPAPIDRNIYVMSEEERIEEGIPSLPADLKEALSELIRSEV
ISDALGDHALAYFYELKEIEWDMYRTQVHQWERDQYLTLY

3D structure

• PDB: 7tdp Molecular dissection of the glutamine synthetase-GlnR nitrogen regulatory circuitry in Gram-positive bacteria.
• Chain: C
• Resolution: 1.98 Å

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	C	G128 E130 E182 D196 Y199 N245 S247 R319 R329	G126 E128 E180 D194 Y197 N243 S245 R317 R327
BS02	P3S	C	E130 E132 E187 E194 G239 H243 R296 E302 R314 R333	E128 E130 E185 E192 G237 H241 R294 E300 R312 R331
BS03	MG	C	E130 E194	E128 E192
BS04	MG	C	E130 H243 E331	E128 H241 E329
BS05	MG	C	E132 E187 E194	E130 E185 E192

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

External links

• PDB: RCSB:7tdp, PDBe:7tdp, PDBj:7tdp
• PDBsum: 7tdp
• PubMed: 35778410
• UniProt: A0A0F0G8G2