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AlphaFold monomer V2.0 prediction for snake venom metalloproteinase trimerelysin-2 (P20165)

Analyse AlphaFold monomer V2.0 prediction for snake venom metalloproteinase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P20165
Type: protein
Length: 201 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x3E2ea5c2D6c6d5995965D85425174aaB4408F9eF
Molecule: Snake venom metalloproteinase trimerelysin-2
UniProt: P20165
Pockets: 1 · best druggability 0.45

Structure

1 distinct chain · 40% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Snake venom metalloproteinase trimerelysin-2	protein	201	40% helix, 16% strand	P20165

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	83	0.45	0.81	24	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1WNI · Crystal structure of H2-proteinase · an experimental structure of the same protein · chain A against A, TM-score 0.97
1WNI · Crystal Structure of H2-Proteinase · an experimental structure of the same protein · chain A against A, TM-score 0.97

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 P20165
Elsewhere: UniProt P20165 · AlphaFold DB P20165

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