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AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (Q59452)

Analyse AlphaFold monomer V2.0 prediction for superoxide dismutase [cu-zn] (Q59452) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q59452
Type: protein
Length: 199 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x83521d6190CB56C500b18eCA10512992858dB9DC
Molecule: Superoxide dismutase [cu-zn]
UniProt: Q59452

Structure

1 distinct chain · 11% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Superoxide dismutase [cu-zn]	protein	199	11% helix, 31% strand	Q59452

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

1Z9N · X-Ray structure of a Cu-Zn superoxide dismutase from Haemophilus ducreyi with haem bound… · an experimental structure of the same protein · chain A against A, TM-score 0.78
1Z9N · X-ray structure of a cu-zn superoxide dismutase from haemophilus ducreyi with haem bound… · an experimental structure of the same protein · chain A against A, TM-score 0.78
1Z9P · X-ray structure of a cu-zn superoxide dismutase from haemophilus ducreyi · an experimental structure of the same protein · chain A against A, TM-score 0.77
1Z9P · X-Ray structure of a Cu-Zn superoxide dismutase from Haemophilus ducreyi · an experimental structure of the same protein · chain A against A, TM-score 0.77

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 Q59452
Elsewhere: UniProt Q59452 · AlphaFold DB Q59452

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