Research workbench
Structure of a bacterial ATM1-family ABC exporter with ATP bound
Analyse Structure of a bacterial ATM1-family ABC exporter with ATP bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PAQ
- Type
- protein
- Length
- 1,134 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATM1-type heavy metal exporter
- UniProt
- Q2G506
- Ligands
- ATP
- Pockets
- 19 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ATM1-type heavy metal exporter | protein | 567 | 63% helix, 10% strand | Q2G506 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1070 | 0.86 | 0.87 | 121 | empty |
| 2 | 496 | 0.82 | 0.89 | 69 | empty |
| 3 | 149 | 0.78 | 0.95 | 36 | empty |
| 4 | 131 | 0.78 | 0.96 | 23 | empty |
| 5 | 442 | 0.74 | 0.84 | 50 | ATP |
Interfaces
1 interface between chains.
- A–B · 7127 Ų buried · 69 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 6PAQ · Structure of a bacterial Atm1-family ABC exporter with ATP bound · the same entry in another collection · chain A against A, TM-score 1.00
- Q2G506 · AlphaFold monomer V2.0 prediction for ATM1-type heavy metal exporter (Q2G506) · a predicted model of the same protein · chain B against A, TM-score 0.85
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 Q2G506
- Elsewhere: RCSB PDB 6PAQ · PDBe 6PAQ · UniProt Q2G506
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