Research workbench
Crystal structure of S-adenosylmethionine synthetase from sulfolobus solfataricus
Analyse Crystal structure of S-adenosylmethionine synthetase from sulfolobus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HPV
- Type
- protein
- Length
- 795 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- S-adenosylmethionine synthase
- EC
- 2.5.1.6
- UniProt
- Q980S9
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-adenosylmethionine synthase (EC 2.5.1.6) | protein | 398 | 35% helix, 30% strand | Q980S9 |
| B | S-adenosylmethionine synthase (EC 2.5.1.6) | protein | 397 | 35% helix, 31% strand | Q980S9 |
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 885 | 0.76 | 0.80 | 85 | empty |
| 2 | 856 | 0.75 | 0.79 | 76 | empty |
| 3 | 389 | 0.74 | 0.85 | 43 | empty |
| 4 | 191 | 0.48 | 0.76 | 20 | empty |
| 5 | 152 | 0.45 | 0.76 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 2449 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 modified (engineered).
Compared structures
- 4HPV · Crystal structure of S-Adenosylmethionine synthetase from Sulfolobus solfataricus · the same entry in another collection · chain A against A, TM-score 1.00
- Q980S9 · AlphaFold monomer V2.0 prediction for S-adenosylmethionine synthase (Q980S9) · a predicted model of the same protein · 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 Q980S9
- Elsewhere: RCSB PDB 4HPV · PDBe 4HPV · UniProt Q980S9
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