Research workbench
Inward facing conformation of the metni methionine ABC transporter
Analyse Inward facing conformation of the metni methionine ABC transporter in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MC0
- Type
- protein
- Length
- 931 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter, permease protein; ABC transporter, ATP-binding protein
- UniProt
- Q9JXP3, Q9JXP2
- Pockets
- 10 · best druggability 0.75
Structure
electron microscopy · 3 distinct chains · 51% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ABC transporter, permease protein | protein | 222 | 82% helix, 1% strand | Q9JXP3 |
| C | ABC transporter, ATP-binding protein | protein | 242 | 39% helix, 21% strand | Q9JXP2 |
| D | ABC transporter, ATP-binding protein | protein | 245 | 36% helix, 20% strand | Q9JXP2 |
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 837 | 0.75 | 0.79 | 64 | empty |
| 2 | 1048 | 0.73 | 0.76 | 92 | empty |
| 3 | 63 | 0.71 | 0.96 | 23 | empty |
| 4 | 72 | 0.63 | 0.91 | 21 | empty |
| 5 | 384 | 0.59 | 0.76 | 34 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1414 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 855 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 842 Ų buried · 11 hydrogen bonds · protein-protein
- C–D · 356 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7MC0 · Inward facing conformation of the MetNI methionine ABC transporter · 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 Q9JXP3
- Every structure of UniProt Q9JXP2
- Elsewhere: RCSB PDB 7MC0 · PDBe 7MC0 · UniProt Q9JXP3 · UniProt Q9JXP2
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