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Methanol tolerant mutant of the proteus mirabilis lipase

Analyse Methanol tolerant mutant of the proteus mirabilis lipase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HS9
Type: protein
Length: 287 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase
EC: 3.1.1.3
UniProt: B4EVM3
Ligands: CA, CL
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipase (EC 3.1.1.3)	protein	287	47% helix, 15% strand	B4EVM3

Ligands and binding sites

CA · Calcium ion · metal · chains A
CL · Chloride ion · ion · chains A
GOL · Glycerol · additive · chains A
1PE · Pentaethylene glycol · additive · chains A
PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · 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	363	0.78	0.87	32	1PE, PE4

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4HS9 · Methanol tolerant mutant of the Proteus mirabilis lipase · 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 B4EVM3
Elsewhere: RCSB PDB 4HS9 · PDBe 4HS9 · UniProt B4EVM3

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