Research workbench
Structure of the complex of proteinase K with a substrate-analogue hexa-peptide inhibitor at 2.2 ångströms resolution
Analyse Structure of the complex of proteinase K with a substrate-analogue hexa-peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PEK
- Type
- protein
- Length
- 285 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteinase K; Peptide pro-ala-pro-phe; D-dal-ala-NH2
- EC
- 3.4.21.64
- UniProt
- P06873
Structure
x-ray diffraction · 3 distinct chains · 27% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Proteinase K (EC 3.4.21.64) | protein | 279 | 27% helix, 23% strand | P06873 |
| C | Peptide pro-ala-pro-phe | protein | 4 | 0% helix, 0% strand | — |
| D | D-dal-ala-NH2 | protein | 2 | 0% helix, 0% strand | — |
Interfaces
3 interfaces between chains.
- E–C · 361 Ų buried · 9 hydrogen bonds · protein-protein
- E–D · 170 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 63 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 2 disulfide, 1 d-amino (disulfide, D-amino acid).
Compared structures
- 1PEK · Structure of the complex of proteinase K with a substrate-analogue hexa-peptide inhibitor… · 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 1PEK · PDBe 1PEK · UniProt P06873
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