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Crystal structure of human pro-granzyme K
Analyse Crystal structure of human pro-granzyme K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MZD
- Type
- protein
- Length
- 240 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pro-granzyme K
- EC
- 3.4.21.-
- UniProt
- P49863
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pro-granzyme K (EC 3.4.21.-) | protein | 240 | 6% helix, 31% strand | P49863 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.51 | 0.77 | 31 | empty |
| 2 | 144 | 0.44 | 0.76 | 30 | empty |
| 3 | 63 | 0.40 | 0.81 | 25 | empty |
Modifications
Observed in the structure: 4 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 P49863
- Elsewhere: RCSB PDB 1MZD · PDBe 1MZD · UniProt P49863
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