Research workbench
Solution NMR structure of the phd domain of human MLL5, northeast structural genomics consortium target HR6512A
Analyse Solution NMR structure of the phd domain of human MLL5, northeast structural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LV9
- Type
- protein
- Length
- 80 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone-lysine N-methyltransferase MLL5
- EC
- 2.1.1.43
- UniProt
- Q8IZD2
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 18% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone-lysine N-methyltransferase MLL5 (EC 2.1.1.43) | protein | 80 | 18% helix, 13% strand | Q8IZD2 |
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
- 2LV9 · Solution NMR structure of the PHD domain of human MLL5, Northeast structural genomics… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8IZD2 · AlphaFold monomer V2.0 prediction for inactive histone-lysine N-methyltransferase 2E… · a predicted model of the same protein · chain A against A, TM-score 0.74
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 Q8IZD2
- Elsewhere: RCSB PDB 2LV9 · PDBe 2LV9 · UniProt Q8IZD2
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