Research workbench

AlphaFold monomer V2.0 prediction for carboxypeptidase D (O75976)

Analyse AlphaFold monomer V2.0 prediction for carboxypeptidase D (O75976) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: O75976
Type: protein
Length: 1,380 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xa468e9aC7533c96f63F5B3a2d6A012D6915744dF
Molecule: Carboxypeptidase D
UniProt: O75976
Pockets: 12 · best druggability 0.72

Structure

1 distinct chain · 29% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carboxypeptidase D	protein	1380	29% helix, 21% strand	O75976

Pockets

12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	768	0.72	0.78	58	empty
2	760	0.68	0.76	55	empty
3	215	0.64	0.83	45	empty
4	217	0.61	0.82	30	empty
5	171	0.59	0.82	21	empty

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

5AQ0 · The structure of the transthyretin-like domain of the first catalytic domain of the human… · an experimental structure of the same protein · chain A against B, TM-score 0.06
5AQ0 · The structure of the Transthyretin-like domain of the first catalytic domain of the HUMAN… · an experimental structure of the same protein · chain A against B, TM-score 0.06

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 O75976
Elsewhere: UniProt O75976 · AlphaFold DB O75976

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