Structure of PDB 1lqw Chain B Binding Site BS01

Receptor Information

>1lqw Chain B (length=183) Species: 1280 (Staphylococcus aureus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

MLTMKDIIRDGHPTLRQKAAELELPLTKEEKETLIAMREFLVNSQDEEIA
KRYGLRSGVGLAAPQINISKRMIAVLIPDDGSGKSYDYMLVNPKIVSHSV
QEAYLPTGEGCLSVDDNVAGLVHRHNRITIKAKDIEGNDIQLRLKGYPAI
VFQHEIDHLNGVMFYDHIDKNHPLQPHTDAVEV

Ligand information

Ligand ID

InChI

InChI=1S/Zn/q+2

InChIKey

PTFCDOFLOPIGGS-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.341	[Zn++]
ACDLabs 10.04 OpenEye OEToolkits 1.5.0	[Zn+2]

Formula

Name

ZINC ION

PDB chain

1lqw Chain B Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

Global view

Local view

Structure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

PDB	1lqw 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.
Resolution	1.87 Å
Binding residue (original residue number in PDB)	C111 H154 H158
Binding residue (residue number reindexed from 1)	C111 H154 H158
Annotation score	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.

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:1lqw, PDBe:1lqw, PDBj:1lqw
PDBsum	1lqw
PubMed	12126617
UniProt	P68826\|DEF_STAAU Peptide deformylase (Gene Name=def)

[Back to BioLiP]