Structure of PDB 1szz Chain D Binding Site BS02

Receptor Information
>1szz Chain D (length=171) Species: 173 (Leptospira interrogans) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SVRKILRMGDPILRKISEPVTEDEIQTKEFKKLIRDMFTTMRHAEGVGLA
APQIGILKQIVVVGSEDNERYPGTPDVPERIILNPVITPLTKDTSGFWEG
CLSVPGMRGYVERPNQIRMQWMDEKGNQFDETIDGYKAIVYQHECDHLQG
ILYVDRLKDTKLFGFNETLDS
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 chain1szz Chain D Residue 516 [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]
PDB1szz Novel conformational states of peptide deformylase from pathogenic bacterium Leptospira interrogans: implications for population shift
Resolution3.3 Å
Binding residue
(original residue number in PDB)		G46 V47 Q53 E99 G100 C101 L102 V140 H143 E144
Binding residue
(residue number reindexed from 1)		G46 V47 Q53 E99 G100 C101 L102 V140 H143 E144
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G48 Q53 C101 L102 H143 E144 H147
Catalytic site (residue number reindexed from 1) G48 Q53 C101 L102 H143 E144 H147
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:0043686 co-translational protein modification

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1szz, PDBe:1szz, PDBj:1szz
PDBsum1szz
PubMed16239225
UniProtQ93LE9|DEF_LEPIN Peptide deformylase (Gene Name=def)

[Back to BioLiP]