MolNFT v1 · #64893 · protein
Crystal structure of the human RAD9-HUS1-RAD1 complex
3GGR: “Crystal structure of the human RAD9-HUS1-RAD1 complex”. X-ray diffraction. MolNFT v1 #64893 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3GGR
- Type
- protein
- Length
- 806 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q99638, O60921, O60671
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 264 | — | Q99638 |
| B | — | protein | 278 | — | O60921 |
| C | — | protein | 264 | — | O60671 |
Compared structures
- 3GGR · Crystal Structure of the Human Rad9-Hus1-Rad1 complex · the same entry in another collection · chain A against A, TM-score 1.00
- O60921 · AlphaFold monomer V2.0 prediction for checkpoint protein HUS1 (O60921) · a predicted model of the same protein · chain B against A, TM-score 0.93
- O60671 · AlphaFold monomer V2.0 prediction for cell cycle checkpoint protein RAD1 (O60671) · a predicted model of the same protein · chain C against A, TM-score 0.92
- Q99638 · AlphaFold monomer V2.0 prediction for cell cycle checkpoint control protein RAD9A (Q99638) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q99638
- Every structure of UniProt O60921
- Every structure of UniProt O60671
- Elsewhere: RCSB PDB 3GGR · PDBe 3GGR · UniProt Q99638 · UniProt O60921 · UniProt O60671
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