Research workbench
1,3-alpha-1,4-beta-D-galactose-4-sulfate- 3,6-anhydro-D-galactose 4 galactohydrolase
Analyse 1,3-alpha-1,4-beta-D-galactose-4-sulfate- 3,6-anhydro-D-galactose 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DYP
- Type
- protein
- Length
- 271 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kappa-carrageenase
- EC
- 3.2.1.83
- UniProt
- P43478
- Ligands
- CD, CL
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kappa-carrageenase (EC 3.2.1.83) | protein | 271 | 5% helix, 53% strand | P43478 |
Ligands and binding sites
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 | 507 | 0.70 | 0.80 | 46 | CD, CL |
Modifications
Observed in the structure: 5 modified, 1 disulfide (engineered, disulfide).
Compared structures
- 1DYP · 1,3-alpha-1,4-beta-D-galactose-4-sulfate-3,6-anhydro-D-galactose 4 galactohydrolase · the same entry in another collection · chain A against A, TM-score 1.00
- P43478 · AlphaFold monomer V2.0 prediction for kappa-carrageenase (P43478) · 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 P43478
- Elsewhere: RCSB PDB 1DYP · PDBe 1DYP · UniProt P43478
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