Research workbench
Cryoem model of copa, the copper transporting ATPase from archaeoglobus fulgidus
Analyse Cryoem model of copa, the copper transporting ATPase from archaeoglobus fulgidus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VOY
- Type
- protein
- Length
- 693 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potential copper-transporting ATPase; SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase…
- EC
- 3.6.3.4, 3.6.3.8
- UniProt
- O32220, P04191, O29777
- Pockets
- 7 · best druggability 0.75
Structure
electron microscopy · 12 distinct chains · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potential copper-transporting ATPase (EC 3.6.3.4) | protein | 80 | 29% helix, 28% strand | O32220 |
| B | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1 (EC 3.6.3.8) | protein | 42 | 55% helix, 0% strand | P04191 |
| C | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1 (EC 3.6.3.8) | protein | 22 | 73% helix, 0% strand | P04191 |
| D | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1 (EC 3.6.3.8) | protein | 23 | 91% helix, 0% strand | P04191 |
| E | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1 (EC 3.6.3.8) | protein | 30 | 47% helix, 0% strand | P04191 |
| F | Cation-transporting ATPase, P-type (EC 3.6.3.4) | protein | 113 | 27% helix, 36% strand | O29777 |
| G | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1 (EC 3.6.3.8) | protein | 36 | 75% helix, 0% strand | P04191 |
| H | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1 (EC 3.6.3.8) | protein | 48 | 58% helix, 4% strand | P04191 |
| I | Cation-transporting ATPase (EC 3.6.3.4) | protein | 128 | 45% helix, 20% strand | — |
| J | Cation-transporting ATPase (EC 3.6.3.4) | protein | 118 | 33% helix, 31% strand | O29777 |
| K | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1 (EC 3.6.3.8) | protein | 32 | 94% helix, 0% strand | P04191 |
| L | SARCOPLASMIC/ENDOPLASMIC reticulum calcium ATPase 1 (EC 3.6.3.8) | protein | 21 | 81% helix, 0% strand | P04191 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 341 | 0.75 | 0.86 | 57 | empty |
| 2 | 983 | 0.73 | 0.77 | 76 | empty |
| 3 | 127 | 0.72 | 0.92 | 25 | empty |
| 4 | 928 | 0.69 | 0.75 | 81 | empty |
| 5 | 115 | 0.41 | 0.75 | 17 | empty |
Interfaces
30 interfaces between chains.
- B–E · 737 Ų buried · 7 hydrogen bonds · protein-protein
- A–F · 728 Ų buried · 49 hydrogen bonds · protein-protein
- B–C · 711 Ų buried · 20 hydrogen bonds · protein-protein
- A–J · 671 Ų buried · 45 hydrogen bonds · protein-protein
- H–K · 670 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 2VOY · CryoEM model of CopA, the copper transporting ATPase from Archaeoglobus fulgidus · the same entry in another collection · chain L against L, TM-score 1.00
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 O32220
- Every structure of UniProt P04191
- Every structure of UniProt O29777
- Elsewhere: RCSB PDB 2VOY · PDBe 2VOY · UniProt O32220 · UniProt P04191 · UniProt O29777
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