MolNFT v1 · #26823 · protein
Crystal structure of E. COLI transhydrogenase domain I with bound NAD
1X14 · NAD(P) transhydrogenase subunit alpha: “Crystal structure of E. COLI transhydrogenase domain I with bound NAD”. X-ray diffraction, 1 ligand (NAD), 7 pockets (best druggability 0.72). MolNFT v1 #26823 on GenesisL1: 3D structure…
- PDB
- 1X14
- Type
- protein
- Length
- 730 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NAD(P) transhydrogenase subunit alpha
- EC
- 1.6.1.2
- UniProt
- P07001
- Ligands
- NAD
- Pockets
- 7 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NAD(P) transhydrogenase subunit alpha (EC 1.6.1.2) | protein | 366 | 40% helix, 17% strand | P07001 |
| B | NAD(P) transhydrogenase subunit alpha (EC 1.6.1.2) | protein | 364 | 38% helix, 17% strand | P07001 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 785 | 0.72 | 0.78 | 77 | empty |
| 2 | 836 | 0.70 | 0.76 | 98 | NAD |
| 3 | 246 | 0.57 | 0.78 | 32 | empty |
| 4 | 179 | 0.48 | 0.76 | 35 | empty |
| 5 | 135 | 0.43 | 0.76 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1633 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 1X14 · Crystal structure of E. coli transhydrogenase domain I with bound NAD · the same entry in another collection · chain A against A, TM-score 1.00
- P07001 · AlphaFold monomer V2.0 prediction for NAD(P) transhydrogenase subunit alpha (P07001) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P07001
- Elsewhere: RCSB PDB 1X14 · PDBe 1X14 · UniProt P07001
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