MolNFT v1 · #44032 · protein
Solution NMR structure of the phd domain of human MLL5, northeast structural genomics consortium target HR6512A
2LV9 · Histone-lysine N-methyltransferase MLL5: “Solution NMR structure of the phd domain of human MLL5, northeast structural genomics consortium target…”. Solution nmr, 1 ligand (ZN). MolNFT v1 #44032 on GenesisL1: 3D structure, binding…
- 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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