Research workbench
Merlin-ferm and LATS1 complex
Analyse Merlin-ferm and LATS1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZRK
- Type
- protein
- Length
- 1,258 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P46662, O95835
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 292 | — | P46662 |
| B, D | — | protein | 293 | — | P46662 |
| C | — | protein | 295 | — | P46662 |
| E, F, H | — | protein | 21 | — | O95835 |
| G | — | protein | 22 | — | O95835 |
Compared structures
- 4ZRK · Merlin-FERM and Lats1 complex · the same entry in another collection · chain H against H, TM-score 1.00
- P46662 · AlphaFold monomer V2.0 prediction for merlin (P46662) · a predicted model of the same protein · chain B against A, TM-score 0.98
- O95835 · AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein kinase LATS1 (O95835) · a predicted model of the same protein · chain G against A, TM-score 0.53
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 P46662
- Every structure of UniProt O95835
- Elsewhere: RCSB PDB 4ZRK · PDBe 4ZRK · UniProt P46662 · UniProt O95835
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