Research workbench
Structure of SMCR8 bound FEM1B
Analyse Structure of SMCR8 bound FEM1B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EL6
- Type
- protein
- Length
- 686 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein fem-1 homolog B,GUANINE nucleotide exchange protein SMCR8
- UniProt
- Q9UK73, Q8TEV9
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein fem-1 homolog B,GUANINE nucleotide exchange protein SMCR8 | protein | 348 | 54% helix, 5% strand | Q9UK73, Q8TEV9 |
| B | Protein fem-1 homolog B,GUANINE nucleotide exchange protein SMCR8 | protein | 338 | 54% helix, 6% strand | Q9UK73, Q8TEV9 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 829 | 0.80 | 0.83 | 93 | empty |
| 2 | 228 | 0.51 | 0.76 | 35 | empty |
| 3 | 50 | 0.40 | 0.82 | 13 | empty |
| 4 | 50 | 0.28 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 980 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7EL6 · Structure of SMCR8 bound FEM1B · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UK73 · AlphaFold monomer V2.0 prediction for protein fem-1 homolog B (Q9UK73) · a predicted model of the same protein · chain B against A, TM-score 0.95
- Q8TEV9 · AlphaFold monomer V2.0 prediction for guanine nucleotide exchange protein SMCR8 (Q8TEV9) · a predicted model of the same protein · chain A against A, TM-score 0.34
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 Q9UK73
- Every structure of UniProt Q8TEV9
- Elsewhere: RCSB PDB 7EL6 · PDBe 7EL6 · UniProt Q9UK73 · UniProt Q8TEV9
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