MolNFT v2 · #118139 · protein
Thermostable aldehyde dehydrogenase from Pyrobaculum sp.1860 complexed with NADP+
5EKC: “Thermostable aldehyde dehydrogenase from Pyrobaculum sp.1860 complexed with NADP+”. X-ray diffraction at 1.895, 1 ligand (NAP). MolNFT v2 #118139 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5EKC
- Type
- protein
- Length
- 3,877 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.895
- Source
- Pyrobaculum sp. 1860
- UniProt
- G7VCG0
- Ligands
- NAP
Structure
x-ray diffraction · resolution 1.895 · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G | — | protein | 484 | — | G7VCG0 |
| B | — | protein | 485 | — | G7VCG0 |
| C | — | protein | 483 | — | G7VCG0 |
| D | — | protein | 484 | — | G7VCG0 |
| E | — | protein | 490 | — | G7VCG0 |
| F | — | protein | 482 | — | G7VCG0 |
| H | — | protein | 485 | — | G7VCG0 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · 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.
Compared structures
- 5EKC · Thermostable aldehyde dehydrogenase from pyrobaculum SP.1860 complexed with NADP+ · 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 G7VCG0
- Elsewhere: RCSB PDB 5EKC · PDBe 5EKC · UniProt G7VCG0
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