Structure of PDB 3u04 Chain A Binding Site BS02

Receptor Information
>3u04 Chain A (length=172) Species: 205920 (Ehrlichia chaffeensis str. Arkansas) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MSVLSIVTVPDKRLSLCSEEVEKVDQSIRKLVDDMFETMHANQGLGLAAV
QVGVHKRILVMNVPEEIEGYELYGGPYCIINPKIVDISQEKVKLKEGCLS
VPGYFDYIVRPQRIAVQYLDYNGNECIIKAQGWLARCLQHEIDHLNGTVF
LKYLSKFKRDFAIEKVKKKERT
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 chain3u04 Chain A Residue 210 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3u04 Crystal structure of peptide deformylase from ehrlichia chaffeensis in complex with actinonin
Resolution1.7 Å
Binding residue
(original residue number in PDB)		G44 L45 G46 Q51 K108 G110 C111 L112 F118 R149 H153 E154 H157
Binding residue
(residue number reindexed from 1)		G44 L45 G46 Q51 K95 G97 C98 L99 F105 R136 H140 E141 H144
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) G46 Q51 C111 L112 H153 E154 H157
Catalytic site (residue number reindexed from 1) G46 Q51 C98 L99 H140 E141 H144
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:3u04, PDBe:3u04, PDBj:3u04
PDBsum3u04
PubMed
UniProtQ2GI30

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