Research workbench
Crystal structure of bmra-E504A in an outward-facing conformation
Analyse Crystal structure of bmra-E504A in an outward-facing conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R72
- Type
- protein
- Length
- 2,277 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multidrug exporter ATP-binding cassette
- UniProt
- A0A164TVX9
- Ligands
- ATP, MG
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 55% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multidrug exporter ATP-binding cassette | protein | 571 | 55% helix, 7% strand | A0A164TVX9 |
| B | Multidrug exporter ATP-binding cassette | protein | 569 | 55% helix, 7% strand | A0A164TVX9 |
| C | Multidrug exporter ATP-binding cassette | protein | 565 | 56% helix, 8% strand | A0A164TVX9 |
| D | Multidrug exporter ATP-binding cassette | protein | 572 | 55% helix, 8% strand | A0A164TVX9 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.83 | 0.93 | 42 | empty |
| 2 | 348 | 0.82 | 0.92 | 39 | empty |
| 3 | 1118 | 0.80 | 0.81 | 119 | empty |
| 4 | 507 | 0.76 | 0.84 | 64 | ATP, MG |
| 5 | 1185 | 0.76 | 0.78 | 95 | empty |
Interfaces
4 interfaces between chains.
- A–B · 7780 Ų buried · 66 hydrogen bonds · protein-protein
- C–D · 7686 Ų buried · 68 hydrogen bonds · protein-protein
- B–C · 295 Ų buried · 2 hydrogen bonds · protein-protein
- B–D · 55 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6R72 · Crystal structure of BmrA-E504A in an outward-facing conformation · the same entry in another collection · chain B against B, 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 A0A164TVX9
- Elsewhere: RCSB PDB 6R72 · PDBe 6R72 · UniProt A0A164TVX9
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