Research workbench

Crystal structure of acylphosphatase from bacillus subtilis

Analyse Crystal structure of acylphosphatase from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BR8
Type: protein
Length: 90 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Probable acylphosphatase
EC: 3.6.1.7
UniProt: O35031
Ligands: PO4

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Probable acylphosphatase (EC 3.6.1.7)	protein	90	27% helix, 40% strand	O35031

Ligands and binding sites

PO4 · Phosphate ion · ion · chains A
GOL · Glycerol · additive · chains A

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

Compared structures

3BR8 · Crystal structure of acylphosphatase from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
O35031 · AlphaFold monomer V2.0 prediction for acylphosphatase (O35031) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 O35031
Elsewhere: RCSB PDB 3BR8 · PDBe 3BR8 · UniProt O35031

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.