Research workbench
Three dimensional structure of porcine pancreatic procarboxypeptidase a. a comparison of the a and B zymogens and their determinants for inhibition and activation
Analyse Three dimensional structure of porcine pancreatic procarboxypeptidase a. a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PCA
- Type
- protein
- Length
- 402 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Procarboxypeptidase a pcpa
- EC
- 3.4.12.2
- UniProt
- P09954
- Ligands
- VAL, ZN
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Procarboxypeptidase a pcpa (EC 3.4.12.2) | protein | 402 | 39% helix, 18% strand | P09954 |
Ligands and binding sites
- VAL · Valine · ligand · chains A
- ZN · Zinc ion · metal · chains A
- CIT · Citric acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.75 | 0.96 | 28 | VAL |
| 2 | 528 | 0.67 | 0.78 | 50 | empty |
| 3 | 65 | 0.38 | 0.79 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1PCA · Three dimensional structure of porcine pancreatic procarboxypeptidase a. a comparison of… · the same entry in another collection · chain A against A, TM-score 1.00
- P09954 · AlphaFold monomer V2.0 prediction for carboxypeptidase A1 (P09954) · a predicted model of the same protein · 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 P09954
- Elsewhere: RCSB PDB 1PCA · PDBe 1PCA · UniProt P09954
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