MolNFT v1 · #248998 · protein
AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator mtrr (P39897)
P39897: “AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator mtrr (P39897)”. 1 pocket (best druggability 0.77). MolNFT v1 #248998 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P39897
- Type
- protein
- Length
- 210 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x91A3Ff8006565B92Be90f7924A65De16701cc9fb
- Molecule
- Hth-type transcriptional regulator mtrr
- UniProt
- P39897
- Pockets
- 1 · best druggability 0.77
Structure
1 distinct chain · 79% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hth-type transcriptional regulator mtrr | protein | 210 | 79% helix, 1% strand | P39897 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 285 | 0.77 | 0.88 | 32 | empty |
Compared structures
- 6OF0 · Structural basis for multidrug recognition and antimicrobial resistance by MTRR, an… · an experimental structure of the same protein · chain A against C, TM-score 0.94
- 6OF0 · Structural basis for multidrug recognition and antimicrobial resistance by mtrr, an… · an experimental structure of the same protein · chain A against C, TM-score 0.94
- 8FW0 · MtrR from Neisseria gonorrhoeae bound to beta-Estradiol · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 8FW8 · MtrR from Neisseria gonorrhoeae bound to Progesterone · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 8FW3 · MtrR from Neisseria gonorrhoeae bound to Testosterone · an experimental structure of the same protein · chain A against A, TM-score 0.91
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 P39897
- Elsewhere: UniProt P39897 · AlphaFold DB P39897
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