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BioLiP

Structure of PDB 4xyc Chain D

Receptor sequence
>4xycD (length=466) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
TEKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGL
AFDGSDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLEPYSRDPRNIA
RKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGSFYEVDAISGWW
NTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDKMLTNLINSGFI
LEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKNTAWQNGKTVTF
MPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDTARHYIGGLLHH
APSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACVRIPITGSNPKA
KRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPVDKDLYELPPEE
AASIPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETWISFKRENEIEP
VNIRPHPYEFALYYDV
3D structure
PDB4xyc Nanomolar inhibitors of Mycobacterium tuberculosis glutamine synthetase 1: Synthesis, biological evaluation and X-ray crystallographic studies.
ChainD
Resolution3.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D50 E129 E131 E215 E223 H272 R343 E362 R364
Catalytic site (residue number reindexed from 1) D53 E121 E123 E207 E215 H264 R335 E354 R356
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 2K9 D Y125 G127 F228 H274 S276 W278 K357 A358 R360 Y117 G119 F220 H266 S268 W270 K349 A350 R352
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
GO:0019740 nitrogen utilization
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane

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Cellular Component
External links
PDB RCSB:4xyc, PDBe:4xyc, PDBj:4xyc
PDBsum4xyc
PubMed25770781
UniProtP9WN38|GLN1B_MYCTO Glutamine synthetase (Gene Name=glnA1)

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