Research workbench
Crystal structure of MTA1-P2 complex
Analyse Crystal structure of MTA1-P2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7F4O
- Type
- protein
- Length
- 346 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transmembrane protein, putative; Mt-A70 family protein
- UniProt
- I7M8B9, Q22GC0
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Transmembrane protein, putative | protein | 129 | 56% helix, 5% strand | I7M8B9 |
| A | Mt-A70 family protein | protein | 217 | 29% helix, 18% strand | Q22GC0 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 136 | 0.59 | 0.83 | 24 | empty |
| 2 | 169 | 0.43 | 0.74 | 27 | empty |
Interfaces
1 interface between chains.
- B–A · 1690 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (engineered).
Compared structures
- 7F4O · Crystal structure of MTA1-p2 complex · 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 I7M8B9
- Every structure of UniProt Q22GC0
- Elsewhere: RCSB PDB 7F4O · PDBe 7F4O · UniProt I7M8B9 · UniProt Q22GC0
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