Research workbench
Crystal structure of the N-terminal domain of SLD7 in complex with SLD3
Analyse Crystal structure of the N-terminal domain of SLD7 in complex with SLD3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3X37
- Type
- protein
- Length
- 243 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ZYRO0C14696P; Mitochondrial morphogenesis protein SLD7
- UniProt
- C5DU83, C5DSD6
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 19% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ZYRO0C14696P | protein | 113 | 15% helix, 26% strand | C5DU83 |
| B | Mitochondrial morphogenesis protein SLD7 | protein | 130 | 22% helix, 45% strand | C5DSD6 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 238 | 0.58 | 0.79 | 29 | empty |
| 2 | 120 | 0.57 | 0.84 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1369 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 3X37 · Crystal structure of the N-terminal domain of Sld7 in complex with Sld3 · the same entry in another collection · chain A against A, TM-score 1.00
- C5DSD6 · AlphaFold monomer V2.0 prediction for mitochondrial morphogenesis protein SLD7 (C5DSD6) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 C5DU83
- Every structure of UniProt C5DSD6
- Elsewhere: RCSB PDB 3X37 · PDBe 3X37 · UniProt C5DU83 · UniProt C5DSD6
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