Research workbench
CFIM25-CFIM68 complex
Analyse CFIM25-CFIM68 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P5T
- Type
- protein
- Length
- 1,653 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O43809, Q16630
Structure
x-ray diffraction · 10 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 196 | — | O43809 |
| B, D | — | protein | 198 | — | O43809 |
| E | — | protein | 191 | — | O43809 |
| F | — | protein | 197 | — | O43809 |
| L | — | protein | 76 | — | Q16630 |
| M | — | protein | 81 | — | Q16630 |
| N | — | protein | 80 | — | Q16630 |
| O | — | protein | 81 | — | Q16630 |
| P | — | protein | 79 | — | Q16630 |
| Q | — | protein | 80 | — | Q16630 |
Compared structures
- 3P5T · CFIm25-CFIm68 complex · the same entry in another collection · chain Q against Q, 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 O43809
- Every structure of UniProt Q16630
- Elsewhere: RCSB PDB 3P5T · PDBe 3P5T · UniProt O43809 · UniProt Q16630
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