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Crystal structure of AED7-norepineprhine complex
Analyse Crystal structure of AED7-norepineprhine complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DYE
- Type
- protein
- Length
- 302 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D7 protein
- UniProt
- P18153
- Ligands
- LNR, BR
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 63% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D7 protein | protein | 302 | 63% helix, 2% strand | P18153 |
Ligands and binding sites
- LNR · L-norepinephrine · ligand · chains A
- BR · Bromide ion · ion · 4 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 334 | 0.71 | 0.83 | 43 | BR, GOL |
| 2 | 53 | 0.70 | 0.98 | 16 | empty |
| 3 | 53 | 0.69 | 0.97 | 16 | LNR |
| 4 | 278 | 0.59 | 0.78 | 29 | empty |
| 5 | 56 | 0.31 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 5 disulfide (disulfide).
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 P18153
- Elsewhere: RCSB PDB 3DYE · PDBe 3DYE · UniProt P18153
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