Research workbench
Crystal structure of S-adenosyl-L-homocysteine hydrolase from acanthamoeba castellanii with bound NAD and adenosine
Analyse Crystal structure of S-adenosyl-L-homocysteine hydrolase from acanthamoeba… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UK3
- Type
- protein
- Length
- 1,900 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- L8H6B5
- Ligands
- NAD, ADN, OXM, K
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 475 | — | L8H6B5 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, C, B, D
- ADN · Adenosine · ligand · 4 copies · chains A, B, C, D
- OXM · Oxamic acid · ligand · chains A
- K · Potassium ion · metal · 4 copies · chains A, B, C, D
- FMT · Formic acid · additive · 9 copies · chains A, D, B, C
- ACT · Acetate ion · additive · 5 copies · chains B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UK3 · Crystal Structure of S-adenosyl-L-homocysteine hydrolase from Acanthamoeba castellanii… · 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 L8H6B5
- Elsewhere: RCSB PDB 6UK3 · PDBe 6UK3 · UniProt L8H6B5
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