Research workbench
Crystal structure of the shroom-binding domain of human ROCK1
Analyse Crystal structure of the shroom-binding domain of human ROCK1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4L2W
- Type
- protein
- Length
- 269 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q13464
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, B | — | protein | 67 | — | Q13464 |
| D | — | protein | 68 | — | Q13464 |
| A | — | protein | 67 | — | Q13464 |
Compared structures
- 4L2W · Crystal structure of the Shroom-Binding domain of human Rock1 · 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 Q13464
- Elsewhere: RCSB PDB 4L2W · PDBe 4L2W · UniProt Q13464
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