Research workbench
Crystal structure of mouse sahh complexed with adenosine
Analyse Crystal structure of mouse sahh complexed with adenosine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5AXA
- Type
- protein
- Length
- 859 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosylhomocysteinase
- EC
- 3.3.1.1
- UniProt
- P50247
- Ligands
- NAD, ADN, NA
- Pockets
- 8 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosylhomocysteinase (EC 3.3.1.1) | protein | 429 | 45% helix, 16% strand | P50247 |
| C | Adenosylhomocysteinase (EC 3.3.1.1) | protein | 430 | 45% helix, 16% strand | P50247 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, C
- ADN · Adenosine · ligand · 2 copies · chains A, C
- NA · Sodium ion · metal · 2 copies · chains A, C
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 | 718 | 0.77 | 0.82 | 92 | NA |
| 2 | 604 | 0.75 | 0.81 | 83 | NAD, ADN |
| 3 | 484 | 0.73 | 0.82 | 63 | NAD, ADN |
| 4 | 269 | 0.56 | 0.76 | 31 | empty |
| 5 | 251 | 0.53 | 0.75 | 32 | empty |
Interfaces
1 interface between chains.
- A–C · 1954 Ų buried · 27 hydrogen bonds · protein-protein
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 P50247
- Elsewhere: RCSB PDB 5AXA · PDBe 5AXA · UniProt P50247
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