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Crystal structure of proglycinin mutant C88S
Analyse Crystal structure of proglycinin mutant C88S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UD1
- Type
- protein
- Length
- 1,098 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycinin G1
- UniProt
- P04776
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Glycinin G1 | protein | 366 | 14% helix, 37% strand | P04776 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 897 | 0.75 | 0.79 | 72 | empty |
| 2 | 122 | 0.42 | 0.76 | 23 | empty |
| 3 | 120 | 0.41 | 0.76 | 24 | empty |
| 4 | 100 | 0.39 | 0.76 | 19 | empty |
| 5 | 60 | 0.33 | 0.77 | 14 | empty |
Interfaces
3 interfaces between chains.
- B–C · 2783 Ų buried · 36 hydrogen bonds · protein-protein
- A–B · 2755 Ų buried · 39 hydrogen bonds · protein-protein
- A–C · 2745 Ų buried · 38 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 P04776
- Elsewhere: RCSB PDB 1UD1 · PDBe 1UD1 · UniProt P04776
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