Research workbench
Crystal structure of reactive loop cleaved kallistatin at 1.9 ångström resolution
Analyse Crystal structure of reactive loop cleaved kallistatin at 1.9 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F4U
- Type
- protein
- Length
- 372 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kallistatin
- UniProt
- P29622
- Ligands
- NA, CL
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kallistatin | protein | 338 | 34% helix, 34% strand | P29622 |
| D | Kallistatin | protein | 34 | 0% helix, 53% strand | P29622 |
Ligands and binding sites
- NA · Sodium ion · metal · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 7 copies · chains A, D
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.40 | 0.75 | 19 | empty |
Interfaces
1 interface between chains.
- A–D · 2463 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 6F4U · Crystal structure of reactive loop cleaved kallistatin at 1.9 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 0.94
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 6F4U · PDBe 6F4U · UniProt P29622
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