Download MendeleyStructural analysis of variants of conjugated bile acid hydrolase from Clostridium perfringens
Rossmann, M., Saenger, W.To be published.
2RG2
Crystal structure of variant R18L of conjugated bile acid hydrolase from Clostridium perfringens
- PDB DOI: https://doi.org/10.2210/pdb2RG2/pdb
- Classification: HYDROLASE
- Organism(s): Clostridium perfringens
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2007-10-02 Released: 2009-02-17
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.213
- R-Value Work: 0.176
- R-Value Observed: 0.178
Starting Model: experimental
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wwPDB Validation 3D Report Full Report
This is version 1.5 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Choloylglycine hydrolase | 328 | Clostridium perfringens | Mutation(s): 1 Gene Names: cbh EC: 3.5.1.24 (PDB Primary Data), 3.5.1 (UniProt), 2.3.1 (UniProt) |  | |
UniProt | |||||
Find proteins for P54965 (Clostridium perfringens (strain 13 / Type A)) Explore P54965 Go to UniProtKB: P54965 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P54965 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SO4 Query on SO4 | B [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | H [auth A], I [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| EDO Query on EDO | C [auth A], D [auth A], E [auth A], F [auth A], G [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| CSO Query on CSO | A | L-PEPTIDE LINKING | C3 H7 N O3 S |  | CYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.213
- R-Value Work: 0.176
- R-Value Observed: 0.178
- Space Group: P 42 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 64.244 | α = 90 |
| b = 64.244 | β = 90 |
| c = 170.023 | γ = 90 |
| Software Name | Purpose |
|---|---|
| DENZO | data reduction |
| SCALEPACK | data scaling |
| REFMAC | refinement |
| PDB_EXTRACT | data extraction |
| HKL-2000 | data collection |
| HKL-2000 | data reduction |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2009-02-17 Deposition Author(s): Rossmann, M., Saenger, W.
Revision History (Full details and data files)
- Version 1.0: 2009-02-17
Type: Initial release - Version 1.1: 2011-07-13
Changes: Non-polymer description, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description - Version 1.3: 2021-10-20
Changes: Database references, Derived calculations - Version 1.4: 2024-04-03
Changes: Data collection, Refinement description - Version 1.5: 2024-10-16
Changes: Structure summary
