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Crystal structure of the catalytic domain of the bacillus cereus sleb protein

Analyse Crystal structure of the catalytic domain of the bacillus cereus sleb protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4F55
Type: protein
Length: 128 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spore cortex-lytic enzyme
UniProt: P0A3V0
Ligands: PO4
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Spore cortex-lytic enzyme	protein	128	45% helix, 9% strand	P0A3V0

Ligands and binding sites

PO4 · Phosphate ion · ion · 3 copies · 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	126	0.37	0.73	20	PO4

Compared structures

4F55 · Crystal Structure of the Catalytic Domain of the Bacillus cereus SleB Protein · the same entry in another collection · chain A against A, TM-score 1.00
P0A3V0 · AlphaFold monomer V2.0 prediction for spore cortex-lytic enzyme (P0A3V0) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P0A3V0
Elsewhere: RCSB PDB 4F55 · PDBe 4F55 · UniProt P0A3V0

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