Research workbench
AlphaFold monomer V2.0 prediction for succinate semialdehyde dehydrogenase [NAD(P)+] sad (P76149)
Analyse AlphaFold monomer V2.0 prediction for succinate semialdehyde dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P76149
- Type
- protein
- Length
- 462 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Succinate semialdehyde dehydrogenase [NAD(P)+] sad
- UniProt
- P76149
- Pockets
- 3 · best druggability 0.68
Structure
1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Succinate semialdehyde dehydrogenase [NAD(P)+] sad | protein | 462 | 43% helix, 21% strand | P76149 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 506 | 0.68 | 0.79 | 57 | empty |
| 2 | 156 | 0.58 | 0.82 | 31 | empty |
| 3 | 113 | 0.41 | 0.76 | 21 | empty |
Compared structures
- 8QMT · Succinic semialdehyde dehydrogenase from E. coli with Q262R substitution and bound NAD+… · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 8QMS · Succinic semialdehyde dehydrogenase from E. coli with Q262R substitution and bound NAD+ · an experimental structure of the same protein · chain A against B, TM-score 0.99
- 8QMR · Succinic semialdehyde dehydrogenase from E. coli with bound NAD+ and succinic semialdehyde · an experimental structure of the same protein · chain A against C, TM-score 0.99
- 8QMQ · Succinic semialdehyde dehydrogenase from E. coli with bound NAD+ · an experimental structure of the same protein · chain A against C, TM-score 0.99
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 P76149
- Elsewhere: UniProt P76149 · AlphaFold DB P76149
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