Download MendeleyCrystal structure of 3-keto-5-aminohexanoate cleavage enzyme (YP_293392.1) from Ralstonia eutropha JMP134 at 1.72 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3C6C
Crystal structure of a putative 3-keto-5-aminohexanoate cleavage enzyme (reut_c6226) from ralstonia eutropha jmp134 at 1.72 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3C6C/pdb
- Classification: HYDROLASE
- Organism(s): Cupriavidus pinatubonensis JMP134
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2008-02-04 Released: 2008-02-19
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.72 Å
- R-Value Free: 0.184
- R-Value Work: 0.153
- R-Value Observed: 0.154
wwPDB Validation 3D Report Full Report
This is version 1.4 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 |
| 3-keto-5-aminohexanoate cleavage enzyme | 316 | Cupriavidus pinatubonensis JMP134 | Mutation(s): 0 Gene Names: YP_293392.1, Reut_C6226 |  | |
UniProt | |||||
Find proteins for Q46MU0 (Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197)) Explore Q46MU0 Go to UniProtKB: Q46MU0 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q46MU0 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| PEG Query on PEG | G [auth A] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N |  | ||
| EDO Query on EDO | D [auth A], E [auth A], F [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| ACT Query on ACT | C [auth A] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| NI Query on NI | B [auth A] | NICKEL (II) ION Ni VEQPNABPJHWNSG-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.72 Å
- R-Value Free: 0.184
- R-Value Work: 0.153
- R-Value Observed: 0.154
- Space Group: I 2 2 2
- Diffraction Data: https://doi.org/10.18430/M33C6C
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 50.339 | α = 90 |
| b = 121.397 | β = 90 |
| c = 133.028 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| SHELX | phasing |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| MAR345 | data collection |
| XDS | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2008-02-19 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2008-02-19
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Source and taxonomy, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description - Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations
