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Crystal structure of peptide deformylase from ehrlichia chaffeensis in complex with actinonin

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

PDB: 3U04
Type: protein
Length: 172 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptide deformylase 1
EC: 3.5.1.88
UniProt: Q2GI30
Ligands: BB2, ZN, CL
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptide deformylase 1 (EC 3.5.1.88)	protein	172	33% helix, 29% strand	Q2GI30

Ligands and binding sites

BB2 · Actinonin · ligand · chains A
ZN · Zinc ion · metal · chains A
CL · Chloride ion · ion · 2 copies · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	119	0.51	0.81	21	BB2
2	55	0.32	0.76	13	empty

Compared structures

3U04 · Crystal structure of peptide deformylase from ehrlichia chaffeensis in complex with… · 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 Q2GI30
Elsewhere: RCSB PDB 3U04 · PDBe 3U04 · UniProt Q2GI30

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