Research workbench

AlphaFold monomer V2.0 prediction for paxillin (Q8VI36)

Analyse AlphaFold monomer V2.0 prediction for paxillin (Q8VI36) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q8VI36
Type: protein
Length: 591 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
Molecule: Paxillin
UniProt: Q8VI36
Pockets: 3 · best druggability 0.49

Structure

1 distinct chain · 19% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Paxillin	protein	591	19% helix, 13% strand	Q8VI36

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	235	0.49	0.74	36	empty
2	73	0.33	0.75	13	empty
3	79	0.31	0.74	16	empty

Compared structures

6JMU · Crystal structure of GIT1/Paxillin complex · an experimental structure of the same protein · chain A against C, TM-score 0.03
6JMU · Crystal structure of GIT1/PAXILLIN complex · an experimental structure of the same protein · chain A against C, TM-score 0.03
5W93 · p130Cas complex with paxillin LD1 · an experimental structure of the same protein · chain A against E, TM-score 0.02
5W93 · P130CAS complex with paxillin LD1 · an experimental structure of the same protein · chain A against E, TM-score 0.02

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 Q8VI36
Elsewhere: UniProt Q8VI36 · AlphaFold DB Q8VI36

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