MolNFT v1 · #190992 · protein
Crystal structure of the R24E mutant of S-adenosyl-L-homocysteine hydrolase from synechocystis sp. pcc 6803 cocrystallized with adenosine in the presence of rb+ cations
7ZD8: “Crystal structure of the R24E mutant of S-adenosyl-L-homocysteine hydrolase from synechocystis sp. pcc 6803…”. X-ray diffraction, 4 ligands (NAD, ADN, RB). MolNFT v1 #190992 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7ZD8
- Type
- protein
- Length
- 831 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P74008
- Ligands
- NAD, ADN, RB, CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 417 | — | P74008 |
| C | — | protein | 414 | — | P74008 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, C
- ADN · Adenosine · ligand · 2 copies · chains A, C
- RB · Rubidium ion · metal · 4 copies · chains A, C
- CL · Chloride ion · ion · 2 copies · chains A, C
- GOL · Glycerol · additive · 4 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7ZD8 · Crystal structure of the R24E mutant of S-adenosyl-L-homocysteine hydrolase from… · the same entry in another collection · chain A against A, TM-score 1.00
- P74008 · AlphaFold monomer V2.0 prediction for adenosylhomocysteinase (P74008) · a predicted model of the same protein · chain C against A, TM-score 0.99
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 P74008
- Elsewhere: RCSB PDB 7ZD8 · PDBe 7ZD8 · UniProt P74008
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.