Research workbench
Crystal structure of activated porcine pancreatic carboxypeptidase B
Analyse Crystal structure of activated porcine pancreatic carboxypeptidase B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z5R
- Type
- protein
- Length
- 912 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Procarboxypeptidase B
- EC
- 3.4.17.2
- UniProt
- P09955
- Ligands
- ZN
- Pockets
- 6 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Procarboxypeptidase B (EC 3.4.17.2) | protein | 304 | 38% helix, 17% strand | P09955 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.64 | 0.84 | 26 | empty |
| 2 | 156 | 0.64 | 0.86 | 24 | empty |
| 3 | 227 | 0.64 | 0.83 | 31 | ZN |
| 4 | 210 | 0.49 | 0.75 | 27 | empty |
| 5 | 90 | 0.41 | 0.78 | 20 | empty |
Interfaces
2 interfaces between chains.
- A–B · 459 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 228 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 disulfide (disulfide).
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 P09955
- Elsewhere: RCSB PDB 1Z5R · PDBe 1Z5R · UniProt P09955
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