Research workbench
Structure of mouse SYCP3, P1 form
Analyse Structure of mouse SYCP3, P1 form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DD9
- Type
- protein
- Length
- 501 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Synaptonemal complex protein 3
- UniProt
- A2RSE7
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 4 distinct chains · 95% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Synaptonemal complex protein 3 | protein | 128 | 94% helix, 0% strand | A2RSE7 |
| B | Synaptonemal complex protein 3 | protein | 127 | 94% helix, 0% strand | A2RSE7 |
| D | Synaptonemal complex protein 3 | protein | 121 | 97% helix, 0% strand | A2RSE7 |
| C | Synaptonemal complex protein 3 | protein | 125 | 97% helix, 0% strand | A2RSE7 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 128 | 0.59 | 0.85 | 22 | empty |
| 2 | 98 | 0.51 | 0.82 | 22 | empty |
| 3 | 54 | 0.31 | 0.76 | 15 | empty |
Interfaces
6 interfaces between chains.
- B–C · 2882 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 2673 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 2619 Ų buried · 9 hydrogen bonds · protein-protein
- D–C · 2475 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 1177 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 28 modified (engineered).
Compared structures
- 6DD9 · Structure of mouse SYCP3, P1 form · 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 A2RSE7
- Elsewhere: RCSB PDB 6DD9 · PDBe 6DD9 · UniProt A2RSE7
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