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Structure of peptide deformylase form helicobacter pylori in complex with actinonin

Analyse Structure of peptide deformylase form helicobacter pylori in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4E9B
Type: protein
Length: 163 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Peptide deformylase 11
EC: 3.5.1.88
UniProt: Q672W7
Ligands: BB2, CO
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptide deformylase 11 (EC 3.5.1.88)	protein	163	33% helix, 28% strand	Q672W7

Ligands and binding sites

BB2 · Actinonin · ligand · chains A
CO · Cobalt (II) ion · metal · chains A
DMS · Dimethyl sulfoxide · additive · 2 copies · chains A
EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	129	0.51	0.80	23	BB2

Compared structures

4E9B · Structure of Peptide Deformylase form Helicobacter Pylori in complex with actinonin · 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 Q672W7
Elsewhere: RCSB PDB 4E9B · PDBe 4E9B · UniProt Q672W7

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