Download MendeleyThe Geometry of the Reactive Site and of the Peptide Groups in Trypsin, Trypsinogen and its Complexes with Inhibitors
Marquart, M., Walter, J., Deisenhofer, J., Bode, W., Huber, R.(1983) Acta Crystallogr B 39: 480
1TPO
THE GEOMETRY OF THE REACTIVE SITE AND OF THE PEPTIDE GROUPS IN TRYPSIN, TRYPSINOGEN AND ITS COMPLEXES WITH INHIBITORS
- PDB DOI: https://doi.org/10.2210/pdb1TPO/pdb
- Classification: HYDROLASE (SERINE PROTEINASE)
- Organism(s): Bos taurus
- Mutation(s): No
- Deposited: 1982-09-27 Released: 1983-01-18
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 ?
- R-Value Work: 0.180
wwPDB Validation 3D Report Full Report
This is version 1.4 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| BETA-TRYPSIN | 223 | Bos taurus | Mutation(s): 0 EC: 3.4.21.4 |  | |
UniProt | |||||
Find proteins for P00760 (Bos taurus) Explore P00760 Go to UniProtKB: P00760 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P00760 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CA Query on CA | B [auth A] | CALCIUM ION Ca BHPQYMZQTOCNFJ-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 ?
- R-Value Work: 0.180
- Space Group: P 21 21 21
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 54.89 | ¦Á = 90 |
| b = 58.52 | ¦Â = 90 |
| c = 67.63 | ¦Ă = 90 |
Entry History
Deposition Data
- Released Date: 1983-01-18 Deposition Author(s): Bode, W., Walter, J., Huber, R.
Revision History (Full details and data files)
- Version 1.0: 1983-01-18
Type: Initial release - Version 1.1: 2008-03-24
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Version format compliance - Version 1.3: 2024-06-05
Changes: Data collection, Database references, Derived calculations, Other - Version 1.4: 2024-10-30
Changes: Structure summary
