Research workbench
Crystal structure of trimeric cre recombinase-lox complex
Analyse Crystal structure of trimeric cre recombinase-lox complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F44
- Type
- protein + DNA
- Length
- 351 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'- D(*TP*AP*TP*AP*AP*CP*TP*TP*CP*GP*TP*AP*TP*AP*GP*C)-3'); DNA (5'…
- UniProt
- P06956
- Pockets
- 6 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 58% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| M | DNA (5'- D(*TP*AP*TP*AP*AP*CP*TP*TP*CP*GP*TP*AP*TP*AP*GP*C)-3') | dna | 16 | — | — |
| N | DNA (5'- D(*AP*TP*AP*TP*GP*CP*TP*AP*TP*AP*CP*GP*AP*AP*GP*TP*TP*AP*T)-3') | dna | 19 | — | — |
| A | Cre recombinase | protein | 316 | 58% helix, 5% strand | P06956 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 499 | 0.69 | 0.80 | 49 | empty |
| 2 | 284 | 0.53 | 0.76 | 27 | empty |
| 3 | 233 | 0.53 | 0.77 | 23 | empty |
| 4 | 167 | 0.51 | 0.79 | 26 | empty |
| 5 | 106 | 0.38 | 0.75 | 16 | empty |
Interfaces
3 interfaces between chains.
- M–A · 1344 Ų buried · 32 hydrogen bonds · protein-nucleic
- N–A · 1254 Ų buried · 39 hydrogen bonds · protein-nucleic
- M–N · 697 Ų buried · 62 hydrogen bonds · nucleic-nucleic
Compared structures
- 1F44 · Crystal structure of trimeric cre recombinase-lox complex · the same entry in another collection · chain M against M, 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 1F44 · PDBe 1F44 · UniProt P06956
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