Research workbench
Alanine dehydrogenase dimer W/BOUND NAD (archaeal)
Analyse Alanine dehydrogenase dimer W/BOUND NAD (archaeal) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OMO
- Type
- protein
- Length
- 640 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alanine dehydrogenase
- EC
- 1.4.1.1
- UniProt
- O28608
- Ligands
- NAD, NA
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Alanine dehydrogenase (EC 1.4.1.1) | protein | 320 | 37% helix, 25% strand | O28608 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 469 | 0.69 | 0.80 | 47 | NAD |
| 2 | 421 | 0.68 | 0.80 | 35 | NAD |
| 3 | 71 | 0.37 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1933 Ų buried · 15 hydrogen bonds · protein-protein
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 O28608
- Elsewhere: RCSB PDB 1OMO · PDBe 1OMO · UniProt O28608
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