Research workbench
Structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase complexed with 5'-methylthiotubercidin
Analyse Structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SD2
- Type
- protein
- Length
- 262 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-methylthioadenosine phosphorylase
- EC
- 2.4.2.28
- UniProt
- Q13126
- Ligands
- MTH, SO4
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5'-methylthioadenosine phosphorylase (EC 2.4.2.28) | protein | 262 | 33% helix, 27% strand | Q13126 |
Ligands and binding sites
- MTH · 2-(4-amino-pyrrolo[2,3-d]pyrimidin-7-yl)-5-methylsulfanylmethyl-tetrahydro-furan-3,4-diol · ligand · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 208 | 0.67 | 0.85 | 28 | SO4, MTH |
| 2 | 70 | 0.32 | 0.74 | 16 | empty |
Compared structures
- 1SD2 · Structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q13126 · AlphaFold monomer V2.0 prediction for S-methyl-5'-thioadenosine phosphorylase (Q13126) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q13126
- Elsewhere: RCSB PDB 1SD2 · PDBe 1SD2 · UniProt Q13126
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