Download MendeleyStructure of Adenylate Kinase 1 in Complex with P1, P4-Di(Adenosine)Tetraphosphate
Bunkoczi, G., Filippakopoulos, P., Jansson, A., Longman, E., von Delft, F., Edwards, A., Arrowsmith, C., Sundstrom, M., Weigelt, J., Knapp, S.To be published.
2C95
Structure of adenylate kinase 1 in complex with P1,P4-di(adenosine) tetraphosphate
- PDB DOI: https://doi.org/10.2210/pdb2C95/pdb
- Classification: TRANSFERASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2005-12-09 Released: 2007-02-20
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.71 Å
- R-Value Free: 0.228
- R-Value Work: 0.176
- R-Value Observed: 0.178
Starting Model: experimental
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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 |
| ADENYLATE KINASE 1 | 196 | Homo sapiens | Mutation(s): 0 EC: 2.7.4.3 (PDB Primary Data), 2.7.4.4 (UniProt), 2.7.4.6 (UniProt) |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P00568 (Homo sapiens) Explore P00568 Go to UniProtKB: P00568 | |||||
PHAROS: P00568 GTEx: ENSG00000106992 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P00568 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| B4P Query on B4P | C [auth A], E [auth B] | BIS(ADENOSINE)-5'-TETRAPHOSPHATE C20 H28 N10 O19 P4 YOAHKNVSNCMZGQ-XPWFQUROSA-N |  | ||
| MLI Query on MLI | D [auth A], F [auth B] | MALONATE ION C3 H2 O4 OFOBLEOULBTSOW-UHFFFAOYSA-L |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.71 Å
- R-Value Free: 0.228
- R-Value Work: 0.176
- R-Value Observed: 0.178
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 62.535 | α = 90 |
| b = 69.998 | β = 90 |
| c = 88.558 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| XDS | data scaling |
| PHASER | phasing |
Entry History
Deposition Data
- Released Date: 2007-02-20 Deposition Author(s): Bunkoczi, G., Filippakopoulos, P., Jansson, A., Longman, E., von Delft, F., Edwards, A., Arrowsmith, C., Sundstrom, M., Knapp, S.
Revision History (Full details and data files)
- Version 1.0: 2007-02-20
Type: Initial release - Version 1.1: 2011-07-13
Changes: Refinement description, Version format compliance - Version 1.2: 2018-01-24
Changes: Database references, Structure summary - Version 1.3: 2018-04-04
Changes: Data collection - Version 1.4: 2023-12-13
Changes: Data collection, Database references, Other, Refinement description
