Research workbench
Crystal structure of human glycosylated kallistatin at 3.0 ångström resolution
Analyse Crystal structure of human glycosylated kallistatin at 3.0 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F02
- Type
- protein
- Length
- 745 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kallistatin
- UniProt
- P29622
- Ligands
- NAG, FUL, BMA, SO4
- Pockets
- 4 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kallistatin | protein | 370 | 29% helix, 30% strand | P29622 |
| C | Kallistatin | protein | 375 | 31% helix, 30% strand | P29622 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A, C
- FUL · beta-L-fucopyranose · sugar · 4 copies · chains A, C
- BMA · beta-D-mannopyranose · sugar · 3 copies · chains C, A
- SO4 · Sulfate ion · ion · 2 copies · chains C, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1069 | 0.76 | 0.78 | 79 | NAG, FUL |
| 2 | 127 | 0.43 | 0.76 | 24 | empty |
| 3 | 89 | 0.37 | 0.76 | 21 | empty |
| 4 | 50 | 0.28 | 0.75 | 10 | empty |
Interfaces
1 interface between chains.
- A–C · 485 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 glycan (N-glycosylation).
Compared structures
- 6F02 · Crystal structure of human glycosylated kallistatin at 3.0 Angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P29622 · AlphaFold monomer V2.0 prediction for kallistatin (P29622) · 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 P29622
- Elsewhere: RCSB PDB 6F02 · PDBe 6F02 · UniProt P29622
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