MolNFT v1 · #48333 · protein
Structure of serine proteinase K complex with a highly flexible hydrophobic peptide at 1.8A resolution
2PQ2: “Structure of serine proteinase K complex with a highly flexible hydrophobic peptide at 1.8A resolution”. X-ray diffraction, 2 ligands (CA, NO3). MolNFT v1 #48333 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2PQ2
- Type
- protein
- Length
- 284 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteinase K; Galag peptide
- 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 |
| B | Galag peptide | 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–B · 322 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2PQ2 · Structure of serine proteinase K complex with a highly flexible hydrophobic peptide at… · 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 2PQ2 · PDBe 2PQ2 · UniProt P06873
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