Structure of PDB 1q1y Chain A

Receptor sequence
>1q1yA (length=186) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
MLTMKDIIRDGHPTLRQKAAELELPLTKEEKETLIAMREFLVNSQDEEIA
KRYGLRSGVGLAAPQINISKRMIAVLIPDDGSGKSYDYMLVNPKIVSHSV
QEAYLPTGEGCLSVDDNVAGLVHRHNRITIKAKDIEGNDIQLRLKGYPAI
VFQHEIDHLNGVMFYDHIDKDHPLQPHTDAVEVLEH
3D structure
PDB1q1y Crystal structure of peptide deformylase from Staphylococcus aureus in complex with actinonin, a naturally occurring antibacterial agent
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) G60 Q65 C111 L112 H154 E155 H158
Catalytic site (residue number reindexed from 1) G60 Q65 C111 L112 H154 E155 H158
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 ZN A A111 H154 H158 A111 H154 H158
BS02 BB2 A R56 S57 G58 V59 G60 Q65 E109 A111 L112 V151 H154 E155 H158 R56 S57 G58 V59 G60 Q65 E109 A111 L112 V151 H154 E155 H158 PDBbind-CN: -logKd/Ki=7.70,IC50=0.02uM
BindingDB: IC50=<5nM
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:1q1y, PDBe:1q1y, PDBj:1q1y
PDBsum1q1y
PubMed15382235
UniProtP68826|DEF_STAAU Peptide deformylase (Gene Name=def)

[Back to BioLiP]