Research workbench
Phd domain of ING4 N214D mutant
Analyse Phd domain of ING4 N214D mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M1R
- Type
- protein
- Length
- 63 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inhibitor of growth protein 4
- UniProt
- Q9UNL4
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 5% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inhibitor of growth protein 4 | protein | 63 | 5% helix, 3% strand | Q9UNL4 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 Q9UNL4
- Elsewhere: RCSB PDB 2M1R · PDBe 2M1R · UniProt Q9UNL4
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