Download MendeleyCrystal structure of ERK2 in complex with a covalently bound macrocyclic ligand
Gelin, M., Labesse, G., Guichou, J.-F., Pons, J.-L., Barluenga, S., Katickeyan, G., Winssinger, N.To be published.
8QR7 | pdb_00008qr7
Crystal structure of ERK2 in complex with a covalently bound macrocyclic ligand
- PDB DOI: https://doi.org/10.2210/pdb8QR7/pdb
- Classification: SIGNALING PROTEIN
- Organism(s): Rattus norvegicus
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2023-10-06 Released: 2025-04-16
- Funding Organization(s): Agence Nationale de la Recherche (ANR)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.51 ?
- R-Value Free: 0.188 (Depositor), 0.188 (DCC)
- R-Value Work: 0.144 (Depositor), 0.144 (DCC)
- R-Value Observed: 0.146 (Depositor)
Starting Model: experimental
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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 |
| Mitogen-activated protein kinase 1 | 364 | Rattus norvegicus | Mutation(s): 0 Gene Names: Mapk1 EC: 2.7.11.24 |  | |
UniProt | |||||
Find proteins for P63086 (Rattus norvegicus) Explore P63086 Go to UniProtKB: P63086 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P63086 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| WMI (Subject of Investigation/LOI) Query on WMI | F [auth A] | (4~{S},9~{S},10~{S})-4-methyl-9,10,16,18-tetrakis(oxidanyl)-3-oxabicyclo[12.4.0]octadeca-1(14),15,17-triene-2,8-dione C18 H24 O7 HLPZXKVMGLUVBS-GNAKQSIWSA-N |  | ||
| SO4 Query on SO4 | B [auth A], C [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| DMS Query on DMS | D [auth A], E [auth A] | DIMETHYL SULFOXIDE C2 H6 O S IAZDPXIOMUYVGZ-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| CME Query on CME | A | L-PEPTIDE LINKING | C5 H11 N O3 S2 |  | CYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.51 ?
- R-Value Free: 0.188 (Depositor), 0.188 (DCC)
- R-Value Work: 0.144 (Depositor), 0.144 (DCC)
- R-Value Observed: 0.146 (Depositor)
Space Group: P 1 21 1
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 48.68 | ¦Á = 90 |
| b = 70.32 | ¦Â = 109.75 |
| c = 60.3 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| Aimless | data scaling |
| MOSFLM | data reduction |
| PHENIX | phasing |
| PHENIX | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-04-16 Deposition Author(s): Gelin, M., Labesse, G.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Agence Nationale de la Recherche (ANR) | France | ANR-20-CE18-0025 |
Revision History (Full details and data files)
- Version 1.0: 2025-04-16
Type: Initial release
