Research workbench
Crystal structure of MEX67-MTR2
Analyse Crystal structure of MEX67-MTR2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OF5
- Type
- protein
- Length
- 282 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MRNA export factor MEX67; MRNA transport regulator MTR2
- UniProt
- Q99257, P34232
- Ligands
- HG
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MRNA export factor MEX67 | protein | 154 | 26% helix, 43% strand | Q99257 |
| B | MRNA transport regulator MTR2 | protein | 128 | 29% helix, 39% strand | P34232 |
Ligands and binding sites
- HG · Mercury (II) ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.42 | 0.83 | 17 | empty |
| 2 | 50 | 0.30 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1360 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1OF5 · Crystal structure of Mex67-Mtr2 · the same entry in another collection · chain A against A, TM-score 1.00
- P34232 · AlphaFold monomer V2.0 prediction for mRNA transport regulator MTR2 (P34232) · a predicted model of the same protein · chain B against A, TM-score 0.97
- Q99257 · AlphaFold monomer V2.0 prediction for mRNA export factor MEX67 (Q99257) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 Q99257
- Every structure of UniProt P34232
- Elsewhere: RCSB PDB 1OF5 · PDBe 1OF5 · UniProt Q99257 · UniProt P34232
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