Research workbench
Structures of the carbinolamine and schiff-base intermediates in the reductive half-reaction of aromatic amine dehydrogenase (aadh) with P-methoxyphenylethylamine
Analyse Structures of the carbinolamine and schiff-base intermediates in the reductive… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HKR
- Type
- protein
- Length
- 952 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aromatic amine dehydrogenase, small subunit; Aromatic amine dehydrogenase, large subunit
- EC
- 1.4.99.4
- UniProt
- Q0VKG6, Q0VKG7
- Ligands
- ZHH, ZHZ
- Pockets
- 8 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D | Aromatic amine dehydrogenase, small subunit (EC 1.4.99.4) | protein | 110 | 8% helix, 37% strand | Q0VKG6 |
| H | Aromatic amine dehydrogenase, small subunit (EC 1.4.99.4) | protein | 122 | 18% helix, 35% strand | Q0VKG6 |
| A, B | Aromatic amine dehydrogenase, large subunit (EC 1.4.99.4) | protein | 360 | 6% helix, 48% strand | Q0VKG7 |
Ligands and binding sites
- ZHH · 2-(4-methoxyphenyl)ethanamine · ligand · chains D, B
- ZHZ · 2-(4-methoxyphenyl)acetamide · ligand · chains H, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 559 | 0.81 | 0.87 | 42 | empty |
| 2 | 546 | 0.80 | 0.86 | 40 | empty |
| 3 | 55 | 0.68 | 0.96 | 18 | ZHZ |
| 4 | 53 | 0.67 | 0.96 | 19 | ZHH |
| 5 | 181 | 0.49 | 0.77 | 35 | empty |
Interfaces
5 interfaces between chains.
- H–A · 1405 Ų buried · 29 hydrogen bonds · protein-protein
- D–B · 1394 Ų buried · 28 hydrogen bonds · protein-protein
- A–B · 929 Ų buried · 18 hydrogen bonds · protein-protein
- H–B · 875 Ų buried · 14 hydrogen bonds · protein-protein
- D–A · 868 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 2 covalent, 2 modified (disulfide, covalent ligand, cofactor).
Compared structures
- 2HKR · Structures of the carbinolamine and schiff-base intermediates in the reductive… · the same entry in another collection · chain D against D, 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 Q0VKG6
- Every structure of UniProt Q0VKG7
- Elsewhere: RCSB PDB 2HKR · PDBe 2HKR · UniProt Q0VKG6 · UniProt Q0VKG7
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