Structure of PDB 4acf Chain F

Receptor sequence
>4acfF (length=475) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
KTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGLAF
DGSSIRGFQSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLEP
YSRDPRNIARKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGSFY
EVDAISGWWNTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDKML
TNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKNTA
WQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDTAR
HYIGGLLHHAPSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACVRI
PITGSNPKAKRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPVDK
DLYELPPEEAASIPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETWIS
FKRENEIEPVNIRPHPYEFALYYDV
3D structure
PDB4acf Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with a Transition-State Mimic Provides Functional Insights.
ChainF
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D54 E133 E135 E219 E227 H276 R347 E366 R368
Catalytic site (residue number reindexed from 1) D51 E130 E132 E216 E224 H273 R344 E363 R365
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 46B F Y129 F232 H278 W282 N359 K361 R364 Y126 F229 H275 W279 N356 K358 R361 PDBbind-CN: -logKd/Ki=5.80,IC50=1.6uM
BS02 MG F E135 E219 E227 E132 E216 E224
BS03 MG F E133 H276 E366 E130 H273 E363
BS04 MG F E133 E227 E130 E224
BS05 P3S F E133 E135 E219 E227 G272 H276 R329 E335 R347 R368 E130 E132 E216 E224 G269 H273 R326 E332 R344 R365
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0001968 fibronectin binding
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0035375 zymogen binding
GO:0046872 metal ion binding
Biological Process
GO:0006542 glutamine biosynthetic process
GO:0010756 positive regulation of plasminogen activation
GO:0019740 nitrogen utilization
GO:0051260 protein homooligomerization
Cellular Component
GO:0005576 extracellular region
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009274 peptidoglycan-based cell wall
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4acf, PDBe:4acf, PDBj:4acf
PDBsum4acf
PubMed
UniProtP9WN39|GLN1B_MYCTU Glutamine synthetase (Gene Name=glnA1)

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