Research workbench
Carboxypeptidase T
Analyse Carboxypeptidase T in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OBR
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Thermoactinomyces vulgaris
- Molecule
- Carboxypeptidase T
- EC
- 3.4.17.18
- UniProt
- P29068
- Ligands
- CA, ZN, SO4
- Pockets
- 2 · best druggability 0.61
Structure
x-ray diffraction · resolution 2.3 · 1 distinct chain · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxypeptidase T (EC 3.4.17.18) | protein | 323 | 35% helix, 17% strand | P29068 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.61 | 0.88 | 24 | SO4 |
| 2 | 52 | 0.27 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 2 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 P29068
- Elsewhere: RCSB PDB 1OBR · PDBe 1OBR · UniProt P29068
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