Structure of PDB 3d2p Chain B Binding Site BS01

Receptor Information
>3d2p Chain B (length=424) Species: 485 (Neisseria gonorrhoeae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DSFVAHFREAAPYIRQMRGTTLVAGIDGRLLEGGTLNKLAADIGLLSQLG
IRLVLIHGAYHFLDRLAAAQGRTPHYCRGLRVTDETSLGQAQQFAGTVRS
RFEAALCGSVSGFARAPSVPLVSGNFLTARPIGVIDGTDMEYAGVIRKTD
TAALRFQLDAGNIVWMPPLGHSYGGKTFNLDMVQAAASVAVSLQAEKLVY
LTLSDGISRPDGTLAETLSAQEAQSLAEHAASETRRLISSAVAALEGGVH
RVQILNGAADGSLLQELFTRNGIGTSIAKEAFVSIRQAHSGDIPHIAALI
RPLILLHRSREYLENHISEFSILEHDGNLYGCAALKTFAEADCGEIACLA
VSPQAQDGGYGERLLAHIIDKARGIGISRLFALSTNTGEWFAERGFQTAS
EDELPETRRKDYRNSHILVRRLHR
Ligand information
Ligand IDCOA
InChIInChI=1S/C21H36N7O16P3S/c1-21(2,16(31)19(32)24-4-3-12(29)23-5-6-48)8-41-47(38,39)44-46(36,37)40-7-11-15(43-45(33,34)35)14(30)20(42-11)28-10-27-13-17(22)25-9-26-18(13)28/h9-11,14-16,20,30-31,48H,3-8H2,1-2H3,(H,23,29)(H,24,32)(H,36,37)(H,38,39)(H2,22,25,26)(H2,33,34,35)/t11-,14-,15-,16+,20-/m1/s1
InChIKeyRGJOEKWQDUBAIZ-IBOSZNHHSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(C)(COP(=O)(O)OP(=O)(O)OCC1C(C(C(O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)C(C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(C)(CO[P@@](O)(=O)O[P@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[C@@H](O)C(=O)NCCC(=O)NCCS
OpenEye OEToolkits 1.5.0CC(C)(CO[P@](=O)(O)O[P@@](=O)(O)OC[C@@H]1[C@H]([C@H]([C@@H](O1)n2cnc3c2ncnc3N)O)OP(=O)(O)O)[C@H](C(=O)NCCC(=O)NCCS)O
CACTVS 3.341CC(C)(CO[P](O)(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O[P](O)(O)=O)n2cnc3c(N)ncnc23)[CH](O)C(=O)NCCC(=O)NCCS
ACDLabs 10.04O=C(NCCS)CCNC(=O)C(O)C(C)(C)COP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3OP(=O)(O)O
FormulaC21 H36 N7 O16 P3 S
NameCOENZYME A
ChEMBLCHEMBL1213327
DrugBankDB01992
ZINCZINC000008551087
PDB chain3d2p Chain B Residue 437 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3d2p Mechanism of Allosteric Inhibition of N-Acetyl-L-glutamate Synthase by L-Arginine.
Resolution2.56 Å
Binding residue
(original residue number in PDB)		L307 L357 V359 Q364 D365 G367 G369 E370 T395 E397 W398
Binding residue
(residue number reindexed from 1)		L303 L349 V351 Q356 D357 G359 G361 E362 T387 E389 W390
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) I30
Catalytic site (residue number reindexed from 1) I26
Enzyme Commision number 2.3.1.1: amino-acid N-acetyltransferase.
Gene Ontology
Molecular Function
GO:0004042 L-glutamate N-acetyltransferase activity
GO:0016746 acyltransferase activity
GO:0016747 acyltransferase activity, transferring groups other than amino-acyl groups
Biological Process
GO:0006526 L-arginine biosynthetic process
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:3d2p, PDBe:3d2p, PDBj:3d2p
PDBsum3d2p
PubMed19095660
UniProtQ5FAK7

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