Research workbench
Structure of the E. COLI macb ABC domain (C2221)
Analyse Structure of the E. COLI macb ABC domain (C2221) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LJ9
- Type
- protein
- Length
- 685 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Macrolide export ATP-BINDING/PERMEASE protein macb
- EC
- 3.6.3.-
- UniProt
- P75831
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Macrolide export ATP-BINDING/PERMEASE protein macb (EC 3.6.3.-) | protein | 229 | 37% helix, 29% strand | P75831 |
| B, C | Macrolide export ATP-BINDING/PERMEASE protein macb (EC 3.6.3.-) | protein | 228 | 37% helix, 29% strand | P75831 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 966 | 0.75 | 0.78 | 97 | empty |
| 2 | 188 | 0.49 | 0.76 | 20 | empty |
| 3 | 146 | 0.46 | 0.77 | 19 | empty |
| 4 | 121 | 0.38 | 0.74 | 25 | empty |
| 5 | 86 | 0.34 | 0.75 | 15 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1303 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 654 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 241 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5LJ9 · Structure of the E. coli MacB ABC domain (C2221) · the same entry in another collection · chain A against A, TM-score 1.00
- P75831 · AlphaFold monomer V2.0 prediction for macrolide export ATP- BINDING/PERMEASE protein macb… · a predicted model of the same protein · chain B 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 P75831
- Elsewhere: RCSB PDB 5LJ9 · PDBe 5LJ9 · UniProt P75831
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