Research workbench
Crystal structure of human S-adenosyl homocysteine hydrolase-like 1 protein
Analyse Crystal structure of human S-adenosyl homocysteine hydrolase-like 1 protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MTG
- Type
- protein
- Length
- 853 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative adenosylhomocysteinase 2
- EC
- 3.3.1.1
- UniProt
- O43865
- Ligands
- NAD
- Pockets
- 8 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative adenosylhomocysteinase 2 (EC 3.3.1.1) | protein | 430 | 42% helix, 16% strand | O43865 |
| B | Putative adenosylhomocysteinase 2 (EC 3.3.1.1) | protein | 423 | 42% helix, 16% strand | O43865 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1053 | 0.84 | 0.84 | 107 | NAD |
| 2 | 423 | 0.75 | 0.84 | 47 | NAD |
| 3 | 112 | 0.63 | 0.87 | 20 | empty |
| 4 | 147 | 0.61 | 0.84 | 24 | empty |
| 5 | 262 | 0.56 | 0.77 | 35 | empty |
Interfaces
1 interface between chains.
- A–B · 2973 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 3MTG · Crystal structure of human S-adenosyl homocysteine hydrolase-like 1 protein · the same entry in another collection · chain A against A, TM-score 1.00
- O43865 · AlphaFold monomer V2.0 prediction for S-adenosylhomocysteine hydrolase-like protein 1… · a predicted model of the same protein · chain B against A, TM-score 0.84
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 O43865
- Elsewhere: RCSB PDB 3MTG · PDBe 3MTG · UniProt O43865
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