Research workbench

Crystal structure of bacillus subtilis lipase at 1.3A resolution

Analyse Crystal structure of bacillus subtilis lipase at 1.3A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ISP
Type: protein
Length: 179 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase
EC: 3.1.1.3
UniProt: P37957

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipase (EC 3.1.1.3)	protein	179	42% helix, 20% strand	P37957

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Compared structures

1ISP · Crystal structure of Bacillus subtilis lipase at 1.3A resolution · the same entry in another collection · chain A against A, TM-score 1.00
P37957 · AlphaFold monomer V2.0 prediction for lipase esta (P37957) · a predicted model of the same protein · 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 P37957
Elsewhere: RCSB PDB 1ISP · PDBe 1ISP · UniProt P37957

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