Research workbench
Crystal structure of dithionite-reduced aromatic amine dehydrogenase (aadh) from alcaligenes faecalis in complex with tryptamine
Analyse Crystal structure of dithionite-reduced aromatic amine dehydrogenase (aadh)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IUQ
- Type
- protein
- Length
- 949 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aromatic amine dehydrogenase alpha subunit; Aromatic amine dehydrogenase beta subunit
- EC
- 1.4.99.4
- Ligands
- TSS
- Pockets
- 7 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 7% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aromatic amine dehydrogenase alpha subunit (EC 1.4.99.4) | protein | 360 | 6% helix, 49% strand | — |
| B | Aromatic amine dehydrogenase alpha subunit (EC 1.4.99.4) | protein | 361 | 6% helix, 48% strand | — |
| D | Aromatic amine dehydrogenase beta subunit (EC 1.4.99.4) | protein | 109 | 8% helix, 32% strand | — |
| H | Aromatic amine dehydrogenase beta subunit (EC 1.4.99.4) | protein | 119 | 11% helix, 29% strand | — |
Ligands and binding sites
- TSS · 2-(1H-indol-3-yl)ethanamine · ligand · 2 copies · chains A, H, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 570 | 0.81 | 0.87 | 44 | empty |
| 2 | 572 | 0.79 | 0.85 | 41 | empty |
| 3 | 52 | 0.68 | 0.96 | 21 | empty |
| 4 | 222 | 0.67 | 0.84 | 37 | TSS |
| 5 | 212 | 0.67 | 0.85 | 35 | TSS |
Interfaces
5 interfaces between chains.
- A–H · 1418 Ų buried · 27 hydrogen bonds · protein-protein
- B–D · 1376 Ų buried · 27 hydrogen bonds · protein-protein
- B–H · 939 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 924 Ų buried · 18 hydrogen bonds · protein-protein
- A–D · 920 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 2 modified (disulfide, cofactor).
Compared structures
- 2IUQ · Crystal structure of dithionite-reduced aromatic amine dehydrogenase (aadh) from… · 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
- Elsewhere: RCSB PDB 2IUQ · PDBe 2IUQ
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