Download MendeleyCrystal structure of Dephospho-CoA kinase (EC 2.7.1.24) (Dephosphocoenzyme A kinase) (tm1387) from THERMOTOGA MARITIMA at 2.60 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
2GRJ
Crystal structure of Dephospho-CoA kinase (EC 2.7.1.24) (Dephosphocoenzyme A kinase) (tm1387) from THERMOTOGA MARITIMA at 2.60 A resolution
- PDB DOI: https://doi.org/10.2210/pdb2GRJ/pdb
- Classification: TRANSFERASE
- Organism(s): Thermotoga maritima
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2006-04-24 Released: 2006-05-23
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Free: 0.245
- R-Value Work: 0.191
- R-Value Observed: 0.193
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 |
| Dephospho-CoA kinase | 192 | Thermotoga maritima | Mutation(s): 4 Gene Names: coaE EC: 2.7.1.24 |  | |
UniProt | |||||
Find proteins for Q9X1A7 (Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)) Explore Q9X1A7 Go to UniProtKB: Q9X1A7 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9X1A7 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| COD Query on COD | BA [auth H] J [auth A] L [auth B] O [auth C] Q [auth D] | DEPHOSPHO COENZYME A C21 H35 N7 O13 P2 S KDTSHFARGAKYJN-IBOSZNHHSA-N |  | ||
| ADP Query on ADP | AA [auth H] I [auth A] K [auth B] N [auth C] P [auth D] | ADENOSINE-5'-DIPHOSPHATE C10 H15 N5 O10 P2 XTWYTFMLZFPYCI-KQYNXXCUSA-N |  | ||
| CL Query on CL | M [auth C], R [auth E], S [auth E], Z [auth H] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A, B, C, D, E A, B, C, D, E, F, G, H | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.60 Å
- R-Value Free: 0.245
- R-Value Work: 0.191
- R-Value Observed: 0.193
- Space Group: P 1 21 1
- Diffraction Data: https://doi.org/10.18430/M32GRJ
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 90.832 | α = 90 |
| b = 87.217 | β = 106.92 |
| c = 98.586 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| XDS | data reduction |
| SHELXD | phasing |
| autoSHARP | phasing |
Entry History
Deposition Data
- Released Date: 2006-05-23 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2006-05-23
Type: Initial release - Version 1.1: 2008-05-01
Changes: Version format compliance - Version 1.2: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.3: 2017-10-25
Changes: Author supporting evidence - Version 1.4: 2023-01-25
Changes: Database references, Derived calculations - Version 1.5: 2024-11-20
Changes: Data collection, Refinement description, Structure summary
