Research workbench
Human dopamine beta-hydroxylase
Analyse Human dopamine beta-hydroxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZEL
- Type
- protein
- Length
- 1,094 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dopamine beta-hydroxylase
- EC
- 1.14.17.1
- UniProt
- P09172
- Ligands
- NAG, BMA, MAN, CU
- Pockets
- 16 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dopamine beta-hydroxylase (EC 1.14.17.1) | protein | 550 | 7% helix, 43% strand | P09172 |
| B | Dopamine beta-hydroxylase (EC 1.14.17.1) | protein | 544 | 6% helix, 44% strand | P09172 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 3 copies
- MAN · alpha-D-mannopyranose · sugar
- CU · Copper (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 425 | 0.72 | 0.83 | 51 | CU |
| 2 | 60 | 0.67 | 0.95 | 19 | empty |
| 3 | 621 | 0.65 | 0.75 | 62 | empty |
| 4 | 233 | 0.63 | 0.82 | 40 | empty |
| 5 | 318 | 0.60 | 0.78 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 1149 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 disulfide, 6 glycan (disulfide, N-glycosylation).
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 P09172
- Elsewhere: RCSB PDB 4ZEL · PDBe 4ZEL · UniProt P09172
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