MolNFT v1 · #22850 · protein

Conformational lability of lipases observed in the absence of an oil-water interface: crystallographic studies of enzymes from the fungi humicola lanuginosa and rhizopus delemar

1TIB: “Conformational lability of lipases observed in the absence of an oil-water interface: crystallographic…”. X-ray diffraction, 2 pockets (best druggability 0.63). MolNFT v1 #22850 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1TIB
Type: protein
Length: 269 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lipase
EC: 3.1.1.3
UniProt: O59952
Pockets: 2 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lipase (EC 3.1.1.3)	protein	269	33% helix, 23% strand	O59952

Pockets

2 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	67	0.63	0.92	22	empty
2	66	0.44	0.82	18	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1TIB · Conformational lability of lipases observed in the absence of an oil-water interface… · 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 1TIB · PDBe 1TIB · UniProt O59952

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