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Crystal structure of porcine pancreatic trypsin with tripeptide inhibitor, pry, at pH 10
Analyse Crystal structure of porcine pancreatic trypsin with tripeptide inhibitor, pry… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XWA
- Type
- protein
- Length
- 224 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trypsin; Acetylated-pro-arg-tyr inhibitor
- EC
- 3.4.21.4
- UniProt
- P00761
- Ligands
- ACE, CA
Structure
x-ray diffraction · 3 distinct chains · 10% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Trypsin (EC 3.4.21.4) | protein | 124 | 2% helix, 40% strand | P00761 |
| B | Trypsin (EC 3.4.21.4) | protein | 98 | 19% helix, 33% strand | P00761 |
| C | Acetylated-pro-arg-tyr inhibitor | protein | 2 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
3 interfaces between chains.
- A–B · 2872 Ų buried · 54 hydrogen bonds · protein-protein
- B–C · 254 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 83 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
- 5XWA · Crystal Structure of Porcine pancreatic trypsin with tripeptide inhibitor, PRY, at pH 10 · 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 P00761
- Elsewhere: RCSB PDB 5XWA · PDBe 5XWA · UniProt P00761
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