Research workbench
Crystal structure of SMAD3-MH1 bound to the ggct site.
Analyse Crystal structure of SMAD3-MH1 bound to the ggct site. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5ODG
- Type
- protein + DNA
- Length
- 277 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P84022
- Ligands
- ZN, CL
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 126 | — | P84022 |
| B | — | protein | 125 | — | P84022 |
| D | — | dna | 13 | — | — |
| E | — | dna | 13 | — | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5ODG · Crystal structure of Smad3-MH1 bound to the GGCT site. · the same entry in another collection · chain A against A, TM-score 1.00
- P84022 · AlphaFold monomer V2.0 prediction for mothers against decapentaplegic homolog 3 (P84022) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P84022
- Elsewhere: RCSB PDB 5ODG · PDBe 5ODG · UniProt P84022
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