Research workbench
Trypsin at pH 4 at atomic resolution
Analyse Trypsin at pH 4 at atomic resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PQ8
- Type
- protein
- Length
- 227 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypsin; Gly-gly-arg peptide
- EC
- 3.4.21.4
- UniProt
- P35049
- Ligands
- LYS, SO4
Structure
x-ray diffraction · 2 distinct chains · 10% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypsin (EC 3.4.21.4) | protein | 224 | 10% helix, 37% strand | P35049 |
| C | Gly-gly-arg peptide | protein | 3 | 0% helix, 0% strand | — |
Ligands and binding sites
- LYS · Lysine · ligand · chains A, C
- SO4 · Sulfate ion · ion · 3 copies · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–C · 312 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent, 3 disulfide (disulfide, covalent ligand, additive adduct).
Compared structures
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 P35049
- Elsewhere: RCSB PDB 1PQ8 · PDBe 1PQ8 · UniProt P35049
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