3SO3
Structures of Fab-Protease Complexes Reveal a Highly Specific Non-Canonical Mechanism of Inhibition.
- PDB DOI: https://doi.org/10.2210/pdb3SO3/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli, Escherichia coli BL21
- Mutation(s): Yes 
- Deposited: 2011-06-29 Released: 2012-06-20 
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.10 Å
- R-Value Free: 0.194 
- R-Value Work: 0.161 
- R-Value Observed: 0.162 
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 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Suppressor of tumorigenicity 14 protein | 241 | Homo sapiens | Mutation(s): 1  Gene Names: PRSS14, SNC19, ST14, TADG15 EC: 3.4.21.109 | ||
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q9Y5Y6 (Homo sapiens) Explore Q9Y5Y6  Go to UniProtKB:  Q9Y5Y6 | |||||
PHAROS:  Q9Y5Y6 GTEx:  ENSG00000149418  | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q9Y5Y6 | ||||
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 |
A11 FAB light chain | 217 | Homo sapiens | Mutation(s): 0  | ||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 3 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
A11 FAB heavy chain | 228 | Homo sapiens | Mutation(s): 0  | ||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
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Oligosaccharides
Small Molecules
Ligands 1 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
GOL Query on GOL | E [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |
Biologically Interesting Molecules (External Reference) 1 Unique
Entity ID: 4 | |||||
---|---|---|---|---|---|
ID | Chains | Name | Type/Class | 2D Diagram | 3D Interactions |
PRD_900003 Query on PRD_900003 | D | sucrose | Oligosaccharide / Nutrient |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.10 Å
- R-Value Free: 0.194 
- R-Value Work: 0.161 
- R-Value Observed: 0.162 
- Space Group: P 64
Unit Cell:
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 130.598 | α = 90 |
b = 130.598 | β = 90 |
c = 96.941 | γ = 120 |
Software Name | Purpose |
---|---|
HKL-2000 | data collection |
PHASER | phasing |
REFMAC | refinement |
StructureStudio | data collection |
SCALA | data scaling |
Entry History 
Deposition Data
- Released Date: 2012-06-20  Deposition Author(s): Schneider, E.L., Farady, C.J., Egea, P.F., Goetz, D.H., Baharuddin, A., Craik, C.S.
Revision History (Full details and data files)
- Version 1.0: 2012-06-20
Type: Initial release - Version 2.0: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Atomic model, Data collection, Database references, Derived calculations, Non-polymer description, Structure summary - Version 2.1: 2023-09-13
Changes: Data collection, Database references, Refinement description, Structure summary