MolNFT v1 · #13627 · protein
Human S-adenosylhomocysteine hydrolase complexed with neplanocin
1LI4: “Human S-adenosylhomocysteine hydrolase complexed with neplanocin”. X-ray diffraction, 2 ligands (NAD, NOC), 7 pockets (best druggability 0.70). MolNFT v1 #13627 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1LI4
- Type
- protein
- Length
- 430 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-adenosylhomocysteine hydrolase
- EC
- 3.3.1.1
- UniProt
- P23526
- Ligands
- NAD, NOC
- Pockets
- 7 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosylhomocysteine hydrolase (EC 3.3.1.1) | protein | 430 | 44% helix, 17% strand | P23526 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A
- NOC · 3-(6-amino-purin-9-yl)-5-hydroxymethyl-cyclopentane-1,2-diol · ligand · chains A
- IPA · Isopropyl alcohol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 482 | 0.70 | 0.81 | 72 | NAD, NOC |
| 2 | 159 | 0.43 | 0.74 | 23 | empty |
| 3 | 72 | 0.37 | 0.77 | 15 | empty |
| 4 | 58 | 0.33 | 0.77 | 10 | empty |
| 5 | 57 | 0.31 | 0.75 | 13 | empty |
Compared structures
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 P23526
- Elsewhere: RCSB PDB 1LI4 · PDBe 1LI4 · UniProt P23526
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