Structure of PDB 1lqy Chain A Binding Site BS01

Receptor Information
>1lqy Chain A (length=184) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MITMKDIIKEGHPTLRKVAEPVPLPPSEEDKRILQSLLDYVKMSQDPELA
AKYGLRPGIGLAAPQINVSKRMIAVHVTDENGTLYSYALFNPKIVSHSVQ
QCYLTTGEGCLSVDRDVPGYVLRYARITVTGTTLDGEEVTLRLKGLPAIV
FQHEIDHLNGIMFYDRINPADPFQVPDGAIPIGR
Ligand information
Ligand IDBB2
InChIInChI=1S/C19H35N3O5/c1-4-5-6-8-14(11-16(24)21-27)18(25)20-17(13(2)3)19(26)22-10-7-9-15(22)12-23/h13-15,17,23,27H,4-12H2,1-3H3,(H,20,25)(H,21,24)/t14-,15+,17+/m1/s1
InChIKeyXJLATMLVMSFZBN-VYDXJSESSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CCCCC[CH](CC(=O)NO)C(=O)N[CH](C(C)C)C(=O)N1CCC[CH]1CO
OpenEye OEToolkits 1.5.0CCCCCC(CC(=O)NO)C(=O)NC(C(C)C)C(=O)N1CCCC1CO
ACDLabs 10.04O=C(N1C(CO)CCC1)C(NC(=O)C(CC(=O)NO)CCCCC)C(C)C
CACTVS 3.341
OpenEye OEToolkits 1.5.0		CCCCC[C@H](CC(=O)NO)C(=O)N[C@@H](C(C)C)C(=O)N1CCC[C@H]1CO
FormulaC19 H35 N3 O5
NameACTINONIN;
2-[(FORMYL-HYDROXY-AMINO)-METHYL]-HEPTANOIC ACID [1-(2-HYDROXYMETHYL-PYRROLIDINE-1-CARBONYL)-2-METHYL-PROPYL]-AMIDE
ChEMBLCHEMBL308333
DrugBankDB04310
ZINCZINC000003979014
PDB chain1lqy Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1lqy The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		G58 I59 G60 Q65 L104 T106 G109 C110 H153 E154 H157
Binding residue
(residue number reindexed from 1)		G58 I59 G60 Q65 L104 T106 G109 C110 H153 E154 H157
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G60 Q65 C110 L111 H153 E154 H157
Catalytic site (residue number reindexed from 1) G60 Q65 C110 L111 H153 E154 H157
Enzyme Commision number 3.5.1.88: peptide deformylase.
Gene Ontology
Molecular Function
GO:0016787 hydrolase activity
GO:0042586 peptide deformylase activity
GO:0046872 metal ion binding
Biological Process
GO:0006412 translation
GO:0018206 peptidyl-methionine modification

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1lqy, PDBe:1lqy, PDBj:1lqy
PDBsum1lqy
PubMed12126617
UniProtO31410|DEF2_GEOSE Peptide deformylase 2

[Back to BioLiP]