1DP5
THE STRUCTURE OF PROTEINASE A COMPLEXED WITH A IA3 MUTANT INHIBITOR
- PDB DOI: https://doi.org/10.2210/pdb1DP5/pdb
- Classification: HYDROLASE/HYDROLASE INHIBITOR
- Organism(s): Saccharomyces cerevisiae
- Expression System: Escherichia coli
- Mutation(s): Yes 
- Deposited: 1999-12-23 Released: 2000-05-03 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.235 
- R-Value Work: 0.188 
wwPDB Validation   3D Report Full Report
This is version 2.1 of the entry. See complete history. 
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
PROTEINASE A | 329 | Saccharomyces cerevisiae | Mutation(s): 0  EC: 3.4.23.25 | ||
UniProt | |||||
Find proteins for P07267 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P07267  Go to UniProtKB:  P07267 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P07267 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
PROTEINASE INHIBITOR IA3 | 68 | Saccharomyces cerevisiae | Mutation(s): 2  | ||
UniProt | |||||
Find proteins for P01094 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P01094  Go to UniProtKB:  P01094 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P01094 | ||||
Sequence AnnotationsExpand | |||||
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Oligosaccharides
Entity ID: 3 | |||||
---|---|---|---|---|---|
Molecule | Chains | Length | 2D Diagram | Glycosylation | 3D Interactions |
beta-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | C | 9 | N-Glycosylation | ||
Glycosylation Resources | |||||
GlyTouCan:  G54269AZ GlyCosmos:  G54269AZ GlyGen:  G54269AZ |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.235 
- R-Value Work: 0.188 
- Space Group: P 62 2 2
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 192.66 | α = 90 |
b = 192.66 | β = 90 |
c = 52.08 | γ = 120 |
Software Name | Purpose |
---|---|
DENZO | data reduction |
SCALEPACK | data scaling |
AMoRE | phasing |
CNS | refinement |
Entry History 
Deposition Data
- Released Date: 2000-05-03  Deposition Author(s): Li, M., Phylip, H.L., Lees, W.E., Winther, J.R., Dunn, B.M., Wlodawer, A., Kay, J., Guschina, A.
Revision History (Full details and data files)
- Version 1.0: 2000-05-03
Type: Initial release - Version 1.1: 2008-04-27
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Non-polymer description, Version format compliance - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Advisory, Atomic model, Data collection, Derived calculations, Structure summary - Version 2.1: 2021-11-03
Changes: Advisory, Database references, Structure summary