Structure of PDB 1jgt Chain B Binding Site BS02

Receptor Information
>1jgt Chain B (length=500) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GAPVLPAAFGFLASARTGGGPGPVFATRGSHTDIDTPQGERSLAATLVHA
PSVAPDRAVARSLTGAPTTAVLAGEIYNRDELLSVLPAGPAPEGDAELVL
RLLERYDLHAFRLVNGRFATVVRTGDRVLLATDHAGSVPLYTCVAPGEVR
ASTEAKALAAHRDPKGFPLADARRVAGLTGVYQVPAGAVMDIDLGSGTAV
THRTWTPGLSRRILPEGEAVAAVRAALEKAVAQRVTPGDTPLVVLSGGID
SSGVAACAHRAAGELDTVSMGTDTSNEFREARAVVDHLRTRHREITIPTT
ELLAQLPYAVWASESVDPDIIEYLLPLTALYRALDGPERRILTGYGADIP
LGGMHREDRLPALDTVLAHDMATFDGLNEMSPVLSTLAGHWTTHPYWDRE
VLDLLVSLEAGLKRRHGRDKWVLRAAMADALPAETVNRPKLSGTTSSFSR
LLLDHGVAEDRVHEAKRQVVRELFDLTVGGGRHPSEVDTDDVVRSVADRT
Ligand information
Ligand IDAPC
InChIInChI=1S/C11H18N5O12P3/c12-9-6-10(14-2-13-9)16(3-15-6)11-8(18)7(17)5(27-11)1-26-29(19,20)4-30(21,22)28-31(23,24)25/h2-3,5,7-8,11,17-18H,1,4H2,(H,19,20)(H,21,22)(H2,12,13,14)(H2,23,24,25)/t5-,7-,8-,11-/m1/s1
InChIKeyCAWZRIXWFRFUQB-IOSLPCCCSA-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)(C[P@](=O)(O)OP(=O)(O)O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)C[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)(CP(=O)(O)OP(=O)(O)O)O)O)O)N
ACDLabs 10.04O=P(O)(O)OP(=O)(O)CP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)C[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
FormulaC11 H18 N5 O12 P3
NameDIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER;
ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL132722
DrugBankDB02596
ZINCZINC000008295117
PDB chain1jgt Chain B Residue 802 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1jgt Structure of beta-lactam synthetase reveals how to synthesize antibiotics instead of asparagine.
Resolution1.95 Å
Binding residue
(original residue number in PDB)		V247 L248 S249 G251 I252 D253 S254 S272 M273 L330 G347 Y348 D351 K423 K443
Binding residue
(residue number reindexed from 1)		V244 L245 S246 G248 I249 D250 S251 S269 M270 L327 G344 Y345 D348 K420 K440
Annotation score3
Enzymatic activity
Catalytic site (original residue number in PDB) A76 G77 D322 Y348 E382 K443
Catalytic site (residue number reindexed from 1) A73 G74 D319 Y345 E379 K440
Enzyme Commision number 6.3.3.4: (carboxyethyl)arginine beta-lactam-synthase.
Gene Ontology
Molecular Function
GO:0004066 asparagine synthase (glutamine-hydrolyzing) activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0034027 (carboxyethyl)arginine beta-lactam-synthase activity
GO:0046872 metal ion binding
Biological Process
GO:0006529 asparagine biosynthetic process
GO:0033050 clavulanic acid biosynthetic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1jgt, PDBe:1jgt, PDBj:1jgt
PDBsum1jgt
PubMed11473258
UniProtP0DJQ7|BLS_STRCL Carboxyethyl-arginine beta-lactam-synthase (Gene Name=bls)

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