MolNFT v1 · #142196 · protein
Covalent bond formation between histidine of vitamin D receptor (vdr) and a full agonist having a enone with a beta methyl group via conjugate addition reaction
5ZWF: “Covalent bond formation between histidine of vitamin D receptor (vdr) and a full agonist having a enone with…”. X-ray diffraction, 1 ligand (9KR). MolNFT v1 #142196 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5ZWF
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P13053
- Ligands
- 9KR
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 237 | — | P13053 |
| C | — | protein | 11 | — | — |
Ligands and binding sites
- 9KR · (E,7R)-7-[(1r,3as,4e,7ar)-7A-methyl-4-[2-[(3R,5R)-4-methylidene-3,5-bis(oxidanyl) cyclohexylidene]ethylidene]-2,3,3A,5,6,7-hexahydro-1H-inden-1-yl]oct-2-en-4-one · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5ZWF · Covalent bond formation between histidine of Vitamin D receptor (VDR) and a full agonist… · the same entry in another collection · chain A against A, TM-score 1.00
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 P13053
- Elsewhere: RCSB PDB 5ZWF · PDBe 5ZWF · UniProt P13053
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