Research workbench
Structures and chemical shift assignments for the add domain of the atrx protein
Analyse Structures and chemical shift assignments for the add domain of the atrx protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LD1
- Type
- protein
- Length
- 142 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcriptional regulator atrx
- EC
- 3.6.4.12
- UniProt
- P46100
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 30% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcriptional regulator atrx (EC 3.6.4.12) | protein | 142 | 30% helix, 11% strand | P46100 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2LD1 · Structures and chemical shift assignments for the ADD domain of the ATRX protein · the same entry in another collection · chain A against A, TM-score 1.00
- P46100 · AlphaFold monomer V2.0 prediction for transcriptional regulator atrx (P46100) · a predicted model of the same protein · chain A against A, TM-score 0.78
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 P46100
- Elsewhere: RCSB PDB 2LD1 · PDBe 2LD1 · UniProt P46100
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