MolNFT v1 · #118622 · protein
Crystal structure of mutant Q289L of ADENOSINE/METHYLTHIOADENOSINE phosphorylase from schistosoma mansoni in complex with adenine
5F7O: “Crystal structure of mutant Q289L of ADENOSINE/METHYLTHIOADENOSINE phosphorylase from schistosoma mansoni in…”. X-ray diffraction, 2 ligands (ADE, SO4), 15 pockets (best druggability 0.86). MolNFT v1 #118622 on GenesisL1: 3D…
- PDB
- 5F7O
- Type
- protein
- Length
- 858 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methylthioadenosine phosphorylase
- EC
- 2.4.2.28
- UniProt
- I0B503
- Ligands
- ADE, SO4
- Pockets
- 15 · best druggability 0.86
Structure
x-ray diffraction · 3 distinct chains · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methylthioadenosine phosphorylase (EC 2.4.2.28) | protein | 286 | 32% helix, 26% strand | I0B503 |
| B | Methylthioadenosine phosphorylase (EC 2.4.2.28) | protein | 285 | 31% helix, 26% strand | I0B503 |
| C | Methylthioadenosine phosphorylase (EC 2.4.2.28) | protein | 287 | 33% helix, 24% strand | I0B503 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 461 | 0.86 | 0.93 | 76 | empty |
| 2 | 411 | 0.78 | 0.86 | 45 | ADE |
| 3 | 185 | 0.74 | 0.90 | 39 | ADE, SO4 |
| 4 | 503 | 0.68 | 0.79 | 51 | SO4 |
| 5 | 138 | 0.48 | 0.78 | 29 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1306 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 1191 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 1086 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 5F7O · Crystal structure of Mutant Q289L of adenosine/Methylthioadenosine phosphorylase from… · 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 I0B503
- Elsewhere: RCSB PDB 5F7O · PDBe 5F7O · UniProt I0B503
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