Research workbench
Complex formed between proteolytically generated lactoferrin fragment and proteinase K
Analyse Complex formed between proteolytically generated lactoferrin fragment and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BJR
- Type
- protein
- Length
- 289 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteinase K; Lactoferrin
- EC
- 3.4.21.64
- UniProt
- P06873
- Ligands
- CA
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Proteinase K (EC 3.4.21.64) | protein | 279 | 28% helix, 23% strand | P06873 |
| I | Lactoferrin | protein | 10 | 0% helix, 0% strand | — |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- E–I · 613 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1BJR · Complex formed between proteolytically generated lactoferrin fragment and proteinase K · the same entry in another collection · chain E against E, 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 P06873
- Elsewhere: RCSB PDB 1BJR · PDBe 1BJR · UniProt P06873
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