Research workbench
Crystal structure of schizosaccharomyces pombe SST2 catalytic domain
Analyse Crystal structure of schizosaccharomyces pombe SST2 catalytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JXE
- Type
- protein
- Length
- 374 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amsh-like protease SST2
- EC
- 3.4.19.-
- UniProt
- Q9P371
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amsh-like protease SST2 (EC 3.4.19.-) | protein | 188 | 23% helix, 31% strand | Q9P371 |
| B | Amsh-like protease SST2 (EC 3.4.19.-) | protein | 186 | 23% helix, 31% strand | Q9P371 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains B
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 | 1011 | 0.86 | 0.86 | 94 | EDO |
Interfaces
1 interface between chains.
- A–B · 758 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 4JXE · Crystal structure of Schizosaccharomyces pombe sst2 catalytic domain · the same entry in another collection · chain A against A, TM-score 1.00
- Q9P371 · AlphaFold monomer V2.0 prediction for amsh-like protease SST2 (Q9P371) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q9P371
- Elsewhere: RCSB PDB 4JXE · PDBe 4JXE · UniProt Q9P371
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