Research workbench
Crystal structure of staphylococcus aureus 5'-METHYLTHIOADENOSINE/S- adenosylhomocysteine nucleosidase
Analyse Crystal structure of staphylococcus aureus 5'-METHYLTHIOADENOSINE/S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GMH
- Type
- protein
- Length
- 230 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-METHYLTHIOADENOSINE/S-adenosylhomocysteine nucleosidase
- EC
- 3.2.2.9
- UniProt
- Q99TQ0
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 5'-METHYLTHIOADENOSINE/S-adenosylhomocysteine nucleosidase (EC 3.2.2.9) | protein | 230 | 38% helix, 30% strand | Q99TQ0 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.62 | 0.87 | 22 | ACT |
Compared structures
- 4GMH · Crystal structure of staphylococcus aureus 5'-methylthioadenosine/s-adenosylhomocysteine… · the same entry in another collection · chain A against A, TM-score 1.00
- Q99TQ0 · AlphaFold monomer V2.0 prediction for 5'-METHYLTHIOADENOSINE/S-adenosylhomocysteine… · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q99TQ0
- Elsewhere: RCSB PDB 4GMH · PDBe 4GMH · UniProt Q99TQ0
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