Download MendeleyCrystal structure of a 5-carboxymethyl-2-hydroxymuconate isomerase from Deinococcus radiodurans R1
Kumaran, D., Almo, S.C., Swaminathan, S.To be published.
4JCU
Crystal structure of a 5-carboxymethyl-2-hydroxymuconate isomerase from Deinococcus radiodurans R1
- PDB DOI: https://doi.org/10.2210/pdb4JCU/pdb
- Classification: ISOMERASE
- Organism(s): Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2013-02-22 Released: 2013-03-13
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.40 Å
- R-Value Free: 0.262
- R-Value Work: 0.204
- R-Value Observed: 0.207
wwPDB Validation 3D Report Full Report
This is version 1.0 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 |
| 5-carboxymethyl-2-hydroxymuconate isomerase | 150 | Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539 | Mutation(s): 0 Gene Names: DR_A0227 |  | |
UniProt | |||||
Find proteins for Q9RYT1 (Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)) Explore Q9RYT1 Go to UniProtKB: Q9RYT1 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9RYT1 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.40 Å
- R-Value Free: 0.262
- R-Value Work: 0.204
- R-Value Observed: 0.207
- Space Group: P 65
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 157.341 | α = 90 |
| b = 157.341 | β = 90 |
| c = 38.197 | γ = 120 |
| Software Name | Purpose |
|---|---|
| CBASS | data collection |
| SHELXD | phasing |
| SHELXE | model building |
| ARP/wARP | model building |
| Coot | model building |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Deposition Data
- Released Date: 2013-03-13 Deposition Author(s): Kumaran, D., Chamala, S., Evans, B., Foti, R., Gizzi, A., Hillerich, B., Kar, A., Lafleur, J., Seidel, R., Villigas, G., Zencheck, W., Al Obaidi, N., Almo, S.C., Swaminathan, S., New York Structural Genomics Research Consortium (NYSGRC)
Revision History (Full details and data files)
- Version 1.0: 2013-03-13
Type: Initial release
