Structure of PDB 1mbz Chain A Binding Site BS03

Receptor Information
>1mbz Chain A (length=496) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APVLPAAFGFLASARTGGPVFATRGSHTDIDTPQGERSLAATLVHAPSVA
PDRAVARSLTGAPTTAVLAGEIYNRDELLSVLPAGPAPEGDAELVLRLLE
RYDLHAFRLVNGRFATVVRTGDRVLLATDHAGSVPLYTCVAPGEVRASTE
AKALAAHGFPLADARRVAGLTGVYQVPAGAVMDIDLGSGTAVTHRTWTPG
LSRRILPEGEAVAAVRAALEKAVAQRVTPGDTPLVVLSGGIDSSGVAACA
HRAAGELDTVSMGTDTSNEFREARAVVDHLRTRHREITIPTTELLAQLPY
AVWASESVDPDIIEYLLPLTALYRALDGPERRILTGYGADIPLGGMHRED
RLPALDTVLAHDMATFDGLNEMSPVLSTLAGHWTTHPYWDREVLDLLVSL
EAGLKRRHGRDKWVLRAAMADALPAETVNRPKLGVHEGSGTTSSFSRLLL
DHGVAEDRVHEAKRQVVRELFDLTVGGGRHPSEVDTDDVVRSVADR
Ligand information
Ligand IDIOT
InChIInChI=1S/C18H28N9O10P/c19-14-11-15(25-6-24-14)27(7-26-11)16-13(30)12(29)9(36-16)5-35-38(33,34)37-10(28)4-23-8(17(31)32)2-1-3-22-18(20)21/h6-9,12-13,16,23,29-30H,1-5H2,(H,31,32)(H,33,34)(H2,19,24,25)(H4,20,21,22)/t8-,9+,12+,13+,16+/m0/s1
InChIKeyPLEMKERVZBXYMR-CWPZRQPOSA-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)OC(=O)CN[C@@H](CCCNC(=N)N)C(=O)O)O)O)N
CACTVS 3.341NC(=N)NCCC[CH](NCC(=O)O[P](O)(=O)OC[CH]1O[CH]([CH](O)[CH]1O)n2cnc3c(N)ncnc23)C(O)=O
ACDLabs 10.04O=C(O)C(NCC(=O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O)CCCNC(=[N@H])N
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OC(=O)CNC(CCCNC(=N)N)C(=O)O)O)O)N
CACTVS 3.341NC(=N)NCCC[C@H](NCC(=O)O[P@@](O)(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1O)n2cnc3c(N)ncnc23)C(O)=O
FormulaC18 H28 N9 O10 P
NameARGININE-N-METHYLCARBONYL PHOSPHORIC ACID 5'-ADENOSINE ESTER
ChEMBL
DrugBank
ZINCZINC000015682440
PDB chain1mbz Chain A Residue 606 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1mbz The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots
Resolution2.47 Å
Binding residue
(original residue number in PDB)		V247 L248 S249 S254 S272 M273 Y326 L330 G347 Y348 G349 D351 I352 D373 E382 K443 G445 V446
Binding residue
(residue number reindexed from 1)		V236 L237 S238 S243 S261 M262 Y315 L319 G336 Y337 G338 D340 I341 D362 E371 K432 G434 V435
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) A76 G77 D322 Y348 E382 K443
Catalytic site (residue number reindexed from 1) A69 G70 D311 Y337 E371 K432
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:1mbz, PDBe:1mbz, PDBj:1mbz
PDBsum1mbz
PubMed12409610
UniProtP0DJQ7|BLS_STRCL Carboxyethyl-arginine beta-lactam-synthase (Gene Name=bls)

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