Structure of PDB 2bvc Chain D Binding Site BS02

Receptor Information
>2bvc Chain D (length=475) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGLAF
DGSSIRGFQSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTLEP
YSRDPRNIARKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGSFY
EVDAISGWWNTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDKML
TNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKNTA
WQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDTAR
HYIGGLLHHAPSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACVRI
PITGSNPKAKRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPVDK
DLYELPPEEAASIPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETWIS
FKRENEIEPVNIRPHPYEFALYYDV
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain2bvc Chain D Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2bvc Structure of Mycobacterium Tuberculosis Glutamine Synthetase in Complex with a Transition-State Mimic Provides Functional Insights.
Resolution2.1 Å
Binding residue
(original residue number in PDB)		E133 E214 K215 N229 Y230 F232 H278 S280 R352 R364
Binding residue
(residue number reindexed from 1)		E130 E211 K212 N226 Y227 F229 H275 S277 R349 R361
Annotation score5
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.
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2bvc, PDBe:2bvc, PDBj:2bvc
PDBsum2bvc
PubMed16027359
UniProtP9WN39|GLN1B_MYCTU Glutamine synthetase (Gene Name=glnA1)

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