Research workbench
Solution structure of the myb-like DNA-binding domain of mouse MTA3 protein
Analyse Solution structure of the myb-like DNA-binding domain of mouse MTA3 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CRG
- Type
- protein
- Length
- 70 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metastasis associated protein MTA3
- UniProt
- Q924K8
Structure
solution nmr · 1 distinct chain · 47% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metastasis associated protein MTA3 | protein | 70 | 47% helix, 0% strand | Q924K8 |
Compared structures
- 2CRG · Solution structure of the myb-like DNA-binding domain of mouse MTA3 protein · the same entry in another collection · chain A against A, TM-score 1.00
- Q924K8 · AlphaFold monomer V2.0 prediction for metastasis-associated protein MTA3 (Q924K8) · a predicted model of the same protein · chain A against A, TM-score 0.64
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 Q924K8
- Elsewhere: RCSB PDB 2CRG · PDBe 2CRG · UniProt Q924K8
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