Research workbench
2.8 ångströms structure of yeast serine carboxypeptidase
Analyse 2.8 ångströms structure of yeast serine carboxypeptidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YSC
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serine carboxypeptidase
- EC
- 3.4.16.5
- UniProt
- P00729
- Ligands
- NAG
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine carboxypeptidase (EC 3.4.16.5) | protein | 421 | 39% helix, 16% strand | P00729 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · 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 | 464 | 0.65 | 0.77 | 50 | empty |
| 2 | 68 | 0.34 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 5 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
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 P00729
- Elsewhere: RCSB PDB 1YSC · PDBe 1YSC · UniProt P00729
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