MolNFT v1 · #107781 · protein
Crystal structure of a zinc-transporting pib-type ATPase in the E2P state
4UMV · Zinc-transporting ATPase: “Crystal structure of a zinc-transporting pib-type ATPase in the E2P state”. X-ray diffraction, 2 ligands (BEF, MG), 10 pockets (best druggability 0.67). MolNFT v1 #107781 on GenesisL1: 3D structure…
- PDB
- 4UMV
- Type
- protein
- Length
- 605 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zinc-transporting ATPase
- EC
- 3.6.3.5
- UniProt
- Q3YW59
- Ligands
- BEF, MG
- Pockets
- 10 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc-transporting ATPase (EC 3.6.3.5) | protein | 605 | 51% helix, 16% strand | Q3YW59 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 306 | 0.67 | 0.82 | 52 | empty |
| 2 | 387 | 0.60 | 0.76 | 63 | empty |
| 3 | 142 | 0.50 | 0.79 | 22 | empty |
| 4 | 186 | 0.46 | 0.75 | 29 | empty |
| 5 | 99 | 0.38 | 0.76 | 19 | empty |
Compared structures
- 4UMV · Crystal structure of a zinc-transporting pib-type ATPase in the E2P state · the same entry in another collection · chain A against A, TM-score 1.00
- Q3YW59 · AlphaFold monomer V2.0 prediction for ZINC/CADMIUM/LEAD-transporting P-type ATPase… · a predicted model of the same protein · chain A against A, TM-score 0.65
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 Q3YW59
- Elsewhere: RCSB PDB 4UMV · PDBe 4UMV · UniProt Q3YW59
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