MolNFT v1 · #26531 · protein

Structure analysis of peptide deformylase from bacillus cereus

1WS1 · Peptide deformylase 1: “Structure analysis of peptide deformylase from bacillus cereus”. X-ray diffraction, 2 ligands (BB2, NI), 1 pocket (best druggability 0.51). MolNFT v1 #26531 on GenesisL1: 3D structure, binding sites and…

PDB: 1WS1
Type: protein
Length: 151 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: Q819U0
Ligands: BB2, NI
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 36% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Peptide deformylase 1 (EC 3.5.1.88)	protein	151	28% helix, 36% strand	Q819U0

Ligands and binding sites

BB2 · Actinonin · ligand · chains A
NI · Nickel (II) 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	126	0.51	0.81	22	BB2

Compared structures

1WS1 · Structure analysis of peptide deformylase from Bacillus cereus · the same entry in another collection · chain A against A, TM-score 1.00
Q819U0 · AlphaFold monomer V2.0 prediction for peptide deformylase 1 (Q819U0) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q819U0
Elsewhere: RCSB PDB 1WS1 · PDBe 1WS1 · UniProt Q819U0

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