Research workbench
Crystal structure of the product synapse complex
Analyse Crystal structure of the product synapse complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C28
- Type
- protein + DNA
- Length
- 682 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Loxp DNA, chain C; Loxp DNA, chain D; Recombinase cre
- UniProt
- P06956
- Pockets
- 11 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 61% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Loxp DNA, chain C | dna | 34 | — | — |
| D | Loxp DNA, chain D | dna | 34 | — | — |
| A | Recombinase cre | protein | 299 | 63% helix, 2% strand | P06956 |
| B | Recombinase cre | protein | 315 | 58% helix, 5% strand | P06956 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1088 | 0.80 | 0.82 | 95 | empty |
| 2 | 307 | 0.64 | 0.81 | 28 | empty |
| 3 | 335 | 0.59 | 0.77 | 29 | empty |
| 4 | 289 | 0.56 | 0.77 | 32 | empty |
| 5 | 245 | 0.50 | 0.75 | 20 | empty |
Interfaces
6 interfaces between chains.
- C–B · 1591 Ų buried · 31 hydrogen bonds · protein-nucleic
- C–D · 1539 Ų buried · 145 hydrogen bonds · nucleic-nucleic
- D–B · 1439 Ų buried · 34 hydrogen bonds · protein-nucleic
- D–A · 1341 Ų buried · 32 hydrogen bonds · protein-nucleic
- A–B · 1256 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 3C28 · Crystal structure of the product synapse complex · the same entry in another collection · chain C against C, 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 P06956
- Elsewhere: RCSB PDB 3C28 · PDBe 3C28 · UniProt P06956
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