MolNFT v1 · #57235 · protein
Crystal structure of the P- and N-domains of copa, a copper- transporting P-type ATPase, bound with ADP-mg
3A1D · Probable copper-exporting P-type ATPase a: “Crystal structure of the P- and N-domains of copa, a copper- transporting P-type ATPase, bound with ADP-mg”. X-ray diffraction, 2 ligands (ADP, MG), 1 pocket (best druggability 0.85).…
- PDB
- 3A1D
- Type
- protein
- Length
- 540 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable copper-exporting P-type ATPase a
- EC
- 3.6.3.-
- UniProt
- O29777
- Ligands
- ADP, MG
- Pockets
- 1 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable copper-exporting P-type ATPase a (EC 3.6.3.-) | protein | 268 | 37% helix, 24% strand | O29777 |
| B | Probable copper-exporting P-type ATPase a (EC 3.6.3.-) | protein | 272 | 38% helix, 24% strand | O29777 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1183 | 0.85 | 0.86 | 142 | ADP, MG |
Interfaces
1 interface between chains.
- A–B · 1140 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 3A1D · Crystal structure of the P- and N-domains of CopA, a copper-transporting P-type ATPase… · the same entry in another collection · chain A against A, TM-score 1.00
- O29777 · AlphaFold monomer V2.0 prediction for probable copper-exporting P-type ATPase (O29777) · a predicted model of the same protein · chain B against A, TM-score 0.67
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 O29777
- Elsewhere: RCSB PDB 3A1D · PDBe 3A1D · UniProt O29777
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