Research workbench
AML1/CBF-BETA/DNA complex
Analyse AML1/CBF-BETA/DNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H9D
- Type
- protein + DNA
- Length
- 544 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q01196, Q13951
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 125 | — | Q01196 |
| B | — | protein | 125 | — | Q13951 |
| D | — | protein | 129 | — | Q13951 |
| E, G | — | dna | 10 | — | — |
| F, H | — | dna | 10 | — | — |
Compared structures
- 1H9D · Aml1/cbf-beta/dna complex · the same entry in another collection · chain H against H, TM-score 1.00
- Q13951 · AlphaFold monomer V2.0 prediction for core-binding factor subunit beta (Q13951) · a predicted model of the same protein · chain B against A, TM-score 0.99
- Q01196 · AlphaFold monomer V2.0 prediction for runt-related transcription factor 1 (Q01196) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q01196
- Every structure of UniProt Q13951
- Elsewhere: RCSB PDB 1H9D · PDBe 1H9D · UniProt Q01196 · UniProt Q13951
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