Research workbench
Crystal structure of an oxidoreductase from agrobacterium radiobacter in complex with NAD+, 2 -hydroxy-2-hydroxymethyl propanoic acid and magnesium
Analyse Crystal structure of an oxidoreductase from agrobacterium radiobacter in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UI9
- Type
- protein
- Length
- 684 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxidoreductase protein
- UniProt
- B9JK80
- Ligands
- NAD, 8A1, MG
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Oxidoreductase protein | protein | 342 | 40% helix, 25% strand | B9JK80 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- 8A1 · (2S)-2,3-dihydroxy-2-methylpropanoic acid · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 524 | 0.74 | 0.82 | 39 | empty |
| 2 | 358 | 0.72 | 0.84 | 50 | NAD, 8A1 |
| 3 | 365 | 0.72 | 0.83 | 52 | NAD, 8A1 |
| 4 | 74 | 0.39 | 0.78 | 18 | empty |
| 5 | 61 | 0.38 | 0.79 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1444 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 5UI9 · Crystal Structure of an Oxidoreductase from Agrobacterium radiobacter in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- B9JK80 · AlphaFold monomer V2.0 prediction for D-apiose dehydrogenase (B9JK80) · a predicted model of the same protein · chain B 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 B9JK80
- Elsewhere: RCSB PDB 5UI9 · PDBe 5UI9 · UniProt B9JK80
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