MolNFT v1 · #160105 · protein
Structure of a bacterial ATM1-family ABC exporter with ATP bound
6PAO · ATM1-type heavy metal exporter: “Structure of a bacterial ATM1-family ABC exporter with ATP bound”. X-ray diffraction, 1 ligand (ATP), 19 pockets (best druggability 0.86). MolNFT v1 #160105 on GenesisL1: 3D structure, binding sites…
- PDB
- 6PAO
- Type
- protein
- Length
- 1,133 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 · 2 distinct chains · 64% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATM1-type heavy metal exporter | protein | 566 | 64% helix, 10% strand | Q2G506 |
| B | ATM1-type heavy metal exporter | protein | 567 | 64% 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, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 946 | 0.86 | 0.88 | 112 | ATP |
| 2 | 1187 | 0.84 | 0.85 | 97 | empty |
| 3 | 630 | 0.78 | 0.83 | 76 | empty |
| 4 | 149 | 0.74 | 0.92 | 34 | empty |
| 5 | 252 | 0.74 | 0.88 | 39 | ATP |
Interfaces
1 interface between chains.
- A–B · 7090 Ų buried · 47 hydrogen bonds · protein-protein
Compared structures
- 6PAO · 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 0.84
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 6PAO · PDBe 6PAO · UniProt Q2G506
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