Structure of PDB 2buf Chain J Binding Site BS01

Receptor Information
>2buf Chain J (length=279) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TLSRDDAAQVAKVLSEALPYIRRFVGKTLVIKYGGNAMESEELKAGFARD
VVLMKAVGINPVVVHGGGPQIGDLLKRLSIESHFIDGMRVTDAATMDVVE
MVLGGQVNKDIVNLINRHGGSAIGLTGKDAELIRAKKLGHVGEVTGVNVG
LLNMLVKGDFIPVIAPIGVGSNGESYNINADLVAGKVAEALKAEKLMLLT
NIAGLMDKQGQVLTGLSTEQVNELIADGTIYGGMLPKIRCALEAVQGGVT
SAHIIDGRVPNAVLLEIFTDSGVGTLISN
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 chain2buf Chain J Residue 1298 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2buf Structural Bases of Feed-Back Control of Arginine Biosynthesis, Revealed by the Structure of Two Hexameric N-Acetylglutamate Kinases, from Thermotoga Maritima and Pseudomonas Aeruginosa
Resolution2.95 Å
Binding residue
(original residue number in PDB)		N37 T218 N219 I220 M224 T247 Y249 M252 K255
Binding residue
(residue number reindexed from 1)		N36 T200 N201 I202 M206 T229 Y231 M234 K237
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K33 G36 G69 D199 K255
Catalytic site (residue number reindexed from 1) K32 G35 G68 D181 K237
Enzyme Commision number 2.7.2.8: acetylglutamate kinase.
Gene Ontology
Molecular Function
GO:0003991 acetylglutamate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0006526 L-arginine biosynthetic process
GO:0016310 phosphorylation
GO:0042450 arginine biosynthetic process via ornithine
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2buf, PDBe:2buf, PDBj:2buf
PDBsum2buf
PubMed16376937
UniProtQ9HTN2|ARGB_PSEAE Acetylglutamate kinase (Gene Name=argB)

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