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Crystal structure of S. aureus peptide deformylase

Analyse Crystal structure of S. aureus peptide deformylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LMH
Type: protein
Length: 184 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (S.AUREUS peptide deformylase)
EC: 3.5.1.27
UniProt: Q9F4L4
Ligands: ZN
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (S.AUREUS peptide deformylase) (EC 3.5.1.27)	protein	184	28% helix, 24% strand	Q9F4L4

Ligands and binding sites

ZN · Zinc ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	142	0.50	0.79	20	ZN

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

1LMH · Crystal Structure of S. aureus peptide deformylase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9F4L4
Elsewhere: RCSB PDB 1LMH · PDBe 1LMH · UniProt Q9F4L4

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