Research workbench

Cutinase, G82A, A85F, V184I, A185L, L189F mutant

Analyse Cutinase, G82A, A85F, V184I, A185L, L189F mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1CUW
Type: protein
Length: 394 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cutinase
EC: 3.1.1.3
UniProt: P00590
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cutinase (EC 3.1.1.3)	protein	197	43% helix, 16% strand	P00590

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	177	0.54	0.79	27	empty
2	81	0.43	0.79	17	empty

Interfaces

1 interface between chains.

A–B · 337 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1CUW · Cutinase, G82A, A85F, V184I, A185L, L189F mutant · the same entry in another collection · chain A against A, TM-score 1.00
P00590 · AlphaFold monomer V2.0 prediction for cutinase 1 (P00590) · a predicted model of the same protein · chain B 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 P00590
Elsewhere: RCSB PDB 1CUW · PDBe 1CUW · UniProt P00590

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