Structure of PDB 1lqy Chain A

Receptor sequence
>1lqyA (length=184) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence]
MITMKDIIKEGHPTLRKVAEPVPLPPSEEDKRILQSLLDYVKMSQDPELA
AKYGLRPGIGLAAPQINVSKRMIAVHVTDENGTLYSYALFNPKIVSHSVQ
QCYLTTGEGCLSVDRDVPGYVLRYARITVTGTTLDGEEVTLRLKGLPAIV
FQHEIDHLNGIMFYDRINPADPFQVPDGAIPIGR
3D structure
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.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 BB2 A G58 I59 G60 Q65 L104 T106 G109 C110 H153 E154 H157 G58 I59 G60 Q65 L104 T106 G109 C110 H153 E154 H157
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

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

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