Research workbench

Crystal structure of aspergillus oryzae cutinase

Analyse Crystal structure of aspergillus oryzae cutinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3GBS
Type: protein
Length: 187 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cutinase 1
EC: 3.1.1.74
UniProt: P52956
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cutinase 1 (EC 3.1.1.74)	protein	187	44% helix, 16% strand	P52956

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	59	0.32	0.76	16	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

3GBS · Crystal structure of Aspergillus oryzae cutinase · the same entry in another collection · chain A against A, TM-score 1.00
P52956 · AlphaFold monomer V2.0 prediction for cutinase 1 (P52956) · 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 P52956
Elsewhere: RCSB PDB 3GBS · PDBe 3GBS · UniProt P52956

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