Research workbench
2.1A crystal structure of the phosphate bound ATP binding domain of archaeoglobus fulgidus copb
Analyse 2.1A crystal structure of the phosphate bound ATP binding domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SKY
- Type
- protein
- Length
- 261 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Copper-exporting P-type ATPase B
- EC
- 3.6.3.4
- UniProt
- O30085
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Copper-exporting P-type ATPase B (EC 3.6.3.4) | protein | 261 | 38% helix, 28% strand | O30085 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- MPO · 3[N-morpholino]propane sulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.35 | 0.75 | 20 | empty |
Compared structures
- 3SKY · 2.1A crystal structure of the phosphate bound ATP binding domain of Archaeoglobus… · the same entry in another collection · chain A against A, TM-score 1.00
- O30085 · AlphaFold monomer V2.0 prediction for copper-exporting P-type ATPase B (O30085) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 O30085
- Elsewhere: RCSB PDB 3SKY · PDBe 3SKY · UniProt O30085
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