Structure of PDB 1mc1 Chain A Binding Site BS03

Receptor Information
>1mc1 Chain A (length=491) Species: 1901 (Streptomyces clavuligerus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VLPAAFGFLASARGPVFATRGSHTDIDTPQGERSLAATLVHAPSVAPDRA
VARSLTGAPTTAVLAGEIYNRDELLSVLPAGPAPEGDAELVLRLLERYDL
HAFRLVNGRFATVVRTGDRVLLATDHAGSVPLYTCVAPGEVRASTEAKAL
AAGFPLADARRVAGLTGVYQVPAGAVMDIDLGSGTAVTHRTWTPGLSRRI
LPEGEAVAAVRAALEKAVAQRVTPGDTPLVVLSGGIDSSGVAACAHRAAG
ELDTVSMGTDTSNEFREARAVVDHLRTRHREITIPTTELLAQLPYAVWAS
ESVDPDIIEYLLPLTALYRALDGPERRILTGYGADIPLGGMHREDRLPAL
DTVLAHDMATFDGLNEMSPVLSTLAGHWTTHPYWDREVLDLLVSLEAGLK
RRHGRDKWVLRAAMADALPAETVNRPKLGVHEGSGTTSSFSRLLLDHGVA
EDRVHEAKRQVVRELFDLTVGGGRHPSEVDTDDVVRSVADR
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 chain1mc1 Chain A Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1mc1 The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots
Resolution2.16 Å
Binding residue
(original residue number in PDB)		V247 S249 S254 S272 M273 G347 K443 V446
Binding residue
(residue number reindexed from 1)		V231 S233 S238 S256 M257 G331 K427 V430
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) A76 G77 D322 Y348 E382 K443
Catalytic site (residue number reindexed from 1) A65 G66 D306 Y332 E366 K427
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:1mc1, PDBe:1mc1, PDBj:1mc1
PDBsum1mc1
PubMed12409610
UniProtP0DJQ7|BLS_STRCL Carboxyethyl-arginine beta-lactam-synthase (Gene Name=bls)

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