Research workbench
Crystal structure of the complex formed between proteinase K and a synthetic peptide leu-leu-phe-asn-asp at 1.67 a resolution
Analyse Crystal structure of the complex formed between proteinase K and a synthetic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DUJ
- Type
- protein
- Length
- 284 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteinase K; Llfnd
- EC
- 3.4.21.64
- UniProt
- P06873
- Ligands
- CA, NO3
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteinase K (EC 3.4.21.64) | protein | 279 | 27% helix, 24% strand | P06873 |
| P | Llfnd | protein | 5 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–P · 413 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2DUJ · Crystal structure of the complex formed between proteinase K and a synthetic peptide… · the same entry in another collection · 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 P06873
- Elsewhere: RCSB PDB 2DUJ · PDBe 2DUJ · UniProt P06873
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