MolNFT v1 · #129643 · protein
PHD2 and winged-helix domain of polycomblike
5OQD: “PHD2 and winged-helix domain of polycomblike”. X-ray diffraction, 2 ligands (ZN, PO4). MolNFT v1 #129643 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OQD
- Type
- protein
- Length
- 1,121 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q24459
- Ligands
- ZN, PO4
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | — | protein | 186 | — | Q24459 |
| A | — | protein | 184 | — | Q24459 |
| C | — | protein | 192 | — | Q24459 |
| D | — | protein | 187 | — | Q24459 |
| E | — | protein | 180 | — | Q24459 |
| F | — | protein | 192 | — | Q24459 |
Ligands and binding sites
- ZN · Zinc ion · metal · 12 copies · chains B, A, C, D, E, F
- PO4 · Phosphate ion · ion · 2 copies · chains C, B, A, D
- EDO · 1,2-ethanediol · additive · 5 copies · chains B, C, F
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 Q24459
- Elsewhere: RCSB PDB 5OQD · PDBe 5OQD · UniProt Q24459
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