Download MendeleyAn arginine tetrad as mediator of input-dependent and input-independent ATPases in the clock protein KaiC
Pattanayek, R., Xu, Y., Lamichhane, A., Johnson, C.H., Egli, M.(2014) Acta Crystallogr D Biol Crystallogr D70: 1375-1390
4O0M
Crystal structure of T. Elongatus BP-1 Clock Protein KaiC
- PDB DOI: https://doi.org/10.2210/pdb4O0M/pdb
- Classification: TRANSFERASE
- Organism(s): Thermosynechococcus vestitus BP-1
- Expression System: Escherichia coli BL21
- Mutation(s): No
- Deposited: 2013-12-13 Released: 2014-05-14
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.84 ?
- R-Value Free: 0.270
- R-Value Work: 0.225
- R-Value Observed: 0.227
This is version 1.1 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Circadian clock protein kinase KaiC | 524 | Thermosynechococcus vestitus BP-1 | Mutation(s): 0 Gene Names: kaiC, tlr0483 EC: 2.7.11.1 (PDB Primary Data), 3.6.4 (UniProt) |  | |
UniProt | |||||
Find proteins for Q79V60 (Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)) Explore Q79V60 Go to UniProtKB: Q79V60 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q79V60 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ATP Query on ATP | E [auth A] F [auth A] I [auth B] K [auth B] M [auth C] | ADENOSINE-5'-TRIPHOSPHATE C10 H16 N5 O13 P3 ZKHQWZAMYRWXGA-KQYNXXCUSA-N |  | ||
| MG Query on MG | D [auth A] G [auth A] H [auth B] J [auth B] L [auth C] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
| Modified Residues 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| SEP Query on SEP | A, B, C | L-PEPTIDE LINKING | C3 H8 N O6 P |  | SER |
| TPO Query on TPO | A, B, C | L-PEPTIDE LINKING | C4 H10 N O6 P |  | THR |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.84 ?
- R-Value Free: 0.270
- R-Value Work: 0.225
- R-Value Observed: 0.227
- Space Group: C 2 2 21
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 130.81 | ¦Á = 90 |
| b = 195.29 | ¦Â = 90 |
| c = 136.64 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| HKL-2000 | data collection |
| PHASER | phasing |
| PHENIX | refinement |
| HKL-2000 | data reduction |
| XSCALE | data scaling |
Entry History
Deposition Data
- Released Date: 2014-05-14 Deposition Author(s): Pattanayek, R., Egli, M.
Revision History (Full details and data files)
- Version 1.0: 2014-05-14
Type: Initial release - Version 1.1: 2024-10-30
Changes: Data collection, Database references, Derived calculations, Structure summary
