Research workbench
Cryo-EM structure of E.COLI mlafeb
Analyse Cryo-EM structure of E.COLI mlafeb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CH7
- Type
- protein
- Length
- 1,214 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipid asymmetry maintenance ABC transporter permease subunit mlae; Phospholipid ABC…
- UniProt
- A0A4S5B3V0, A0A4V3YUQ9, A0A4S5B5E3
- Pockets
- 17 · best druggability 0.80
Structure
electron microscopy · 3 distinct chains · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Lipid asymmetry maintenance ABC transporter permease subunit mlae | protein | 248 | 78% helix, 0% strand | A0A4S5B3V0 |
| C, D | Phospholipid ABC transporter ATP-binding protein mlaf | protein | 265 | 34% helix, 17% strand | A0A4V3YUQ9 |
| E, F | Lipid asymmetry maintenance protein mlab | protein | 94 | 33% helix, 18% strand | A0A4S5B5E3 |
Pockets
17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 416 | 0.80 | 0.88 | 56 | empty |
| 2 | 362 | 0.67 | 0.81 | 47 | empty |
| 3 | 427 | 0.66 | 0.79 | 47 | empty |
| 4 | 217 | 0.61 | 0.81 | 33 | empty |
| 5 | 258 | 0.60 | 0.79 | 33 | empty |
Interfaces
8 interfaces between chains.
- C–D · 1978 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 1816 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 930 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 924 Ų buried · 12 hydrogen bonds · protein-protein
- D–F · 791 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 7CH7 · Cryo-EM structure of E.coli MlaFEB · the same entry in another collection · chain A against A, 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 A0A4S5B3V0
- Every structure of UniProt A0A4V3YUQ9
- Every structure of UniProt A0A4S5B5E3
- Elsewhere: RCSB PDB 7CH7 · PDBe 7CH7 · UniProt A0A4S5B3V0 · UniProt A0A4V3YUQ9 · UniProt A0A4S5B5E3
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