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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).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CProcarboxypeptidase B (EC 3.4.17.2)protein30438% helix, 17% strandP09955

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12010.640.8426empty
21560.640.8624empty
32270.640.8331ZN
42100.490.7527empty
5900.410.7820empty

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

  • 1Z5R · Crystal Structure of Activated Porcine Pancreatic Carboxypeptidase B · the same entry in another collection · chain A against A, TM-score 1.00
  • P09955 · AlphaFold monomer V2.0 prediction for carboxypeptidase B (P09955) · a predicted model of the same protein · chain A against A, TM-score 1.00

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