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AlphaFold monomer V2.0 prediction for 5'-3' exonuclease PLD3 (O35405)

Analyse AlphaFold monomer V2.0 prediction for 5'-3' exonuclease PLD3 (O35405) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: O35405
Type: protein
Length: 488 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
Molecule: 5'-3' exonuclease PLD3
UniProt: O35405
Pockets: 3 · best druggability 0.56

Structure

1 distinct chain · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	5'-3' exonuclease PLD3	protein	488	35% helix, 24% strand	O35405

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	275	0.56	0.77	35	empty
2	186	0.52	0.78	34	empty
3	56	0.29	0.75	19	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

8V05 · Crystal structure of mouse PLD3 · an experimental structure of the same protein · chain A against A, TM-score 0.85
8V06 · Crystal structure of mouse PLD3 co-crystallized with 5'Pi-ssDNA for 9 days · an experimental structure of the same protein · chain A against B, TM-score 0.84
8V07 · Crystal structure of mouse PLD3 co-crystallized with 5'Pi-ssDNA for 30 days · an experimental structure of the same protein · chain A against A, TM-score 0.83

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 O35405
Elsewhere: UniProt O35405 · AlphaFold DB O35405

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