Research workbench
Atomic resolution crystal structures of kallikrein-related peptidase 4 complexed with sunflower trypsin inhibitor (sfti-1)
Analyse Atomic resolution crystal structures of kallikrein-related peptidase 4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K8Y
- Type
- protein
- Length
- 236 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Kallikrein-4; Trypsin inhibitor 1
- EC
- 3.4.21.-
- UniProt
- Q9Y5K2, Q4GWU5
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Kallikrein-4 (EC 3.4.21.-) | protein | 223 | 12% helix, 36% strand | Q9Y5K2 |
| B | Trypsin inhibitor 1 | protein | 13 | 0% helix, 31% strand | Q4GWU5 |
Interfaces
1 interface between chains.
- A–B · 680 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 4K8Y · Atomic resolution crystal structures of Kallikrein-Related Peptidase 4 complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9Y5K2 · AlphaFold monomer V2.0 prediction for kallikrein-4 (Q9Y5K2) · a predicted model of the same protein · chain A against A, TM-score 1.00
- Q4GWU5 · AlphaFold monomer V2.0 prediction for trypsin inhibitor 1 (Q4GWU5) · a predicted model of the same protein · chain B against A, TM-score 0.44
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 Q9Y5K2
- Every structure of UniProt Q4GWU5
- Elsewhere: RCSB PDB 4K8Y · PDBe 4K8Y · UniProt Q9Y5K2 · UniProt Q4GWU5
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