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AlphaFold monomer V2.0 prediction for ribulose bisphosphate CARBOXYLASE/OXYGENASE activase 1, chloroplastic (Q7X9A0)

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

Accession: Q7X9A0
Type: protein
Length: 476 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x1613987cbC1744e137dAE77F5F9ad3696140470F
Molecule: Ribulose bisphosphate CARBOXYLASE/OXYGENASE activase 1, chloroplastic
UniProt: Q7X9A0
Pockets: 3 · best druggability 0.55

Structure

1 distinct chain · 40% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ribulose bisphosphate CARBOXYLASE/OXYGENASE activase 1, chloroplastic	protein	476	40% helix, 7% strand	Q7X9A0

Pockets

3 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	244	0.55	0.77	32	empty
2	83	0.33	0.74	24	empty
3	53	0.28	0.74	14	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3THG · Crystal structure of the creosote Rubisco activase C-domain · an experimental structure of the same protein · chain A against A, TM-score 0.17
3THG · Crystal structure of the creosote rubisco activase C-domain · an experimental structure of the same protein · chain A against A, TM-score 0.17

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 Q7X9A0
Elsewhere: UniProt Q7X9A0 · AlphaFold DB Q7X9A0

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