MolNFT v1 · #541771 · protein
AlphaFold monomer V2.0 prediction for ZINC/CADMIUM/LEAD-transporting P-type ATPase (P37617)
P37617: “AlphaFold monomer V2.0 prediction for ZINC/CADMIUM/LEAD-transporting P-type ATPase (P37617)”. 7 pockets (best druggability 0.81). MolNFT v1 #541771 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- P37617
- Type
- protein
- Length
- 732 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xfe3404c48e7625928d3baDED30F60435478de73c
- Molecule
- ZINC/CADMIUM/LEAD-transporting P-type ATPase
- UniProt
- P37617
- Pockets
- 7 · best druggability 0.81
Structure
1 distinct chain · 50% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ZINC/CADMIUM/LEAD-transporting P-type ATPase | protein | 732 | 50% helix, 19% strand | P37617 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1088 | 0.81 | 0.82 | 87 | empty |
| 2 | 523 | 0.62 | 0.75 | 50 | empty |
| 3 | 291 | 0.54 | 0.76 | 33 | empty |
| 4 | 92 | 0.39 | 0.77 | 19 | empty |
| 5 | 66 | 0.33 | 0.75 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1MWZ · Solution structure of the N-terminal domain of ZntA in the Zn(II)-form · an experimental structure of the same protein · chain A against A, TM-score 0.09
- 1MWZ · Solution structure of the N-terminal domain of znta in the ZN(II)-form · an experimental structure of the same protein · chain A against A, TM-score 0.09
- 1MWY · Solution structure of the N-terminal domain of ZntA in the apo-form · an experimental structure of the same protein · chain A against A, TM-score 0.09
- 1MWY · Solution structure of the N-terminal domain of znta in the apo-form · an experimental structure of the same protein · chain A against A, TM-score 0.09
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 P37617
- Elsewhere: UniProt P37617 · AlphaFold DB P37617
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