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Crystal structure of fungal lipase from THERMOMYCES(HUMICOLA) lanuginosa at 2.30 ångström resolution.

Analyse Crystal structure of fungal lipase from THERMOMYCES(HUMICOLA) lanuginosa at… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EA6
Type: protein
Length: 538 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase
EC: 3.1.1.3
UniProt: O59952
Pockets: 4 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Lipase (EC 3.1.1.3)	protein	269	31% helix, 24% strand	O59952

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	215	0.58	0.79	40	empty
2	83	0.35	0.76	19	empty
3	86	0.34	0.75	20	empty
4	59	0.29	0.74	17	empty

Interfaces

1 interface between chains.

A–B · 600 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

4EA6 · Crystal structure of Fungal lipase from Thermomyces(Humicola) lanuginosa at 2.30 Angstrom… · the same entry in another collection · chain A against A, TM-score 1.00
O59952 · AlphaFold monomer V2.0 prediction for lipase (O59952) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O59952
Elsewhere: RCSB PDB 4EA6 · PDBe 4EA6 · UniProt O59952

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