Research workbench
Crystal structure of the DNA-binding domain of human CHD1.
Analyse Crystal structure of the DNA-binding domain of human CHD1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4B4C
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chromodomain-helicase-DNA-binding protein 1
- EC
- 3.6.4.12
- UniProt
- O14646
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 58% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chromodomain-helicase-DNA-binding protein 1 (EC 3.6.4.12) | protein | 187 | 58% helix, 4% strand | O14646 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4B4C · Crystal structure of the DNA-binding domain of human CHD1. · the same entry in another collection · chain A against A, TM-score 1.00
- O14646 · AlphaFold monomer V2.0 prediction for chromodomain-helicase-DNA- binding protein 1… · 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 O14646
- Elsewhere: RCSB PDB 4B4C · PDBe 4B4C · UniProt O14646
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