Structure of PDB 1hto Chain T Binding Site BS02

Receptor Information
>1hto Chain T (length=477) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TEKTPDDVFKLAKDEKVEYVDVRFCDLPGIMQHFTIPASAFDKSVFDDGL
AFDGSSIRGFQSIHESDMLLLPDPETARIDPFRAAKTLNINFFVHDPFTL
EPYSRDPRNIARKAENYLISTGIADTAYFGAEAEFYIFDSVSFDSRANGS
FYEVDAISGWWNTGAATEADGSPNRGYKVRHKGGYFPVAPNDQYVDLRDK
MLTNLINSGFILEKGHHEVGSGGQAEINYQFNSLLHAADDMQLYKYIIKN
TAWQNGKTVTFMPKPLFGDNGSGMHCHQSLWKDGAPLMYDETGYAGLSDT
ARHYIGGLLHHAPSLLAFTNPTVNSYKRLVPGYEAPINLVYSQRNRSACV
RIPITGSNPKAKRLEFRSPDSSGNPYLAFSAMLMAGLDGIKNKIEPQAPV
DKDLYELPPEEAASIPQTPTQLSDVIDRLEADHEYLTEGGVFTNDLIETW
ISFKRENEIEPVNIRPHPYEFALYYDV
Ligand information
Ligand IDAMP
InChIInChI=1S/C10H14N5O7P/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(22-10)1-21-23(18,19)20/h2-4,6-7,10,16-17H,1H2,(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyUDMBCSSLTHHNCD-KQYNXXCUSA-N
SMILES
SoftwareSMILES
CACTVS 3.370Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(O)=O)[CH](O)[CH]3O
CACTVS 3.370Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)O)O)O)N
ACDLabs 12.01O=P(O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.7.6c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)O)O)O)N
FormulaC10 H14 N5 O7 P
NameADENOSINE MONOPHOSPHATE
ChEMBLCHEMBL752
DrugBankDB00131
ZINCZINC000003860156
PDB chain1hto Chain T Residue 7513 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1hto Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		Y125 G127 E129 F225 H271 S273 R355
Binding residue
(residue number reindexed from 1)		Y128 G130 E132 F231 H277 S279 R363
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D50 E129 E131 E212 E220 H269 R339 E357 R359
Catalytic site (residue number reindexed from 1) D53 E132 E134 E218 E226 H275 R346 E365 R367
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
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Biological Process
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Cellular Component
External links
PDB RCSB:1hto, PDBe:1hto, PDBj:1hto
PDBsum1hto
PubMed12146952
UniProtP9WN39|GLN1B_MYCTU Glutamine synthetase (Gene Name=glnA1)

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