Research workbench
P. syringae alda indole-3-acetaldehyde dehydrogenase C302A mutant in complex with NAD+ and iaa
Analyse P. syringae alda indole-3-acetaldehyde dehydrogenase C302A mutant in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JSO
- Type
- protein
- Length
- 3,960 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldehyde dehydrogenase family protein
- UniProt
- Q88BC5
- Ligands
- NAI, IAC
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Aldehyde dehydrogenase family protein | protein | 495 | 44% helix, 21% strand | Q88BC5 |
Ligands and binding sites
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- IAC · 1H-indol-3-ylacetic acid · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 286 | 0.83 | 0.94 | 44 | empty |
| 2 | 294 | 0.83 | 0.94 | 42 | empty |
| 3 | 290 | 0.82 | 0.93 | 42 | empty |
| 4 | 1099 | 0.82 | 0.83 | 95 | NAI, IAC |
| 5 | 699 | 0.81 | 0.86 | 73 | empty |
Interfaces
9 interfaces between chains.
- B–D · 2597 Ų buried · 56 hydrogen bonds · protein-protein
- A–C · 2576 Ų buried · 55 hydrogen bonds · protein-protein
- E–H · 2543 Ų buried · 56 hydrogen bonds · protein-protein
- G–H · 1023 Ų buried · 10 hydrogen bonds · protein-protein
- E–G · 947 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 covalent (covalent ligand).
Compared structures
- 7JSO · P. syringae AldA Indole-3-Acetaldehyde Dehydrogenase C302A mutant in complex with NAD+… · 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 Q88BC5
- Elsewhere: RCSB PDB 7JSO · PDBe 7JSO · UniProt Q88BC5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.