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Crystal structure of bacillus licheniformis lipase BLEST2 in propetide form

Analyse Crystal structure of bacillus licheniformis lipase BLEST2 in propetide form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WPX
Type: protein
Length: 901 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BLEST2
UniProt: A0A415J7C9
Ligands: IOD
Pockets: 7 · best druggability 0.72

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BLEST2	protein	450	27% helix, 33% strand	A0A415J7C9
B	BLEST2	protein	451	27% helix, 33% strand	A0A415J7C9

Ligands and binding sites

IOD · Iodide ion · ion · 24 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	737	0.72	0.78	71	IOD
2	247	0.62	0.81	31	IOD
3	259	0.58	0.78	34	IOD
4	184	0.54	0.79	29	IOD
5	55	0.50	0.86	16	IOD

Interfaces

1 interface between chains.

A–B · 257 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6WPX · Crystal structure of Bacillus licheniformis lipase BlEst2 in propetide form · 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 A0A415J7C9
Elsewhere: RCSB PDB 6WPX · PDBe 6WPX · UniProt A0A415J7C9

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