Download MendeleyThe crystal structure of the N-terminal domain of MdmX in complex with p53p peptide fragment
Cheng, X.Y., Zhang, B.L., Li, Z.C., Kuang, Z.K., Su, Z.D.To be published.
7EL4 | pdb_00007el4
The crystal structure of p53p peptide fragment in complex with the N-terminal domain of MdmX
- PDB DOI: https://doi.org/10.2210/pdb7EL4/pdb
- Classification: ONCOPROTEIN
- Organism(s): Homo sapiens
- Expression System: Escherichia coli K-12
- Mutation(s): No
- Deposited: 2021-04-08 Released: 2021-06-09
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.11 Å
- R-Value Free: 0.225 (Depositor), 0.250 (DCC)
- R-Value Work: 0.224 (Depositor), 0.220 (DCC)
Starting Model: experimental
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This is version 1.1 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 |
| Cellular tumor antigen p53,Protein Mdm4 | 130 | Homo sapiens | Mutation(s): 0 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for O15151 (Homo sapiens) Explore O15151 Go to UniProtKB: O15151 | |||||
PHAROS: O15151 GTEx: ENSG00000198625 | |||||
Find proteins for P04637 (Homo sapiens) Explore P04637 Go to UniProtKB: P04637 | |||||
PHAROS: P04637 GTEx: ENSG00000141510 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Groups | O15151P04637 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| O4B Query on O4B | B [auth A], C [auth A] | 1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE C12 H24 O6 XEZNGIUYQVAUSS-UHFFFAOYSA-N |  | ||
| MG Query on MG | D [auth A], E [auth A] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.11 Å
- R-Value Free: 0.225 (Depositor), 0.250 (DCC)
- R-Value Work: 0.224 (Depositor), 0.220 (DCC)
Space Group: I 41
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 65.097 | α = 90 |
| b = 65.097 | β = 90 |
| c = 94.977 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data collection |
| autoPROC | data processing |
| XDS | data reduction |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
Entry History
Deposition Data
- Released Date: 2021-06-09 Deposition Author(s): Cheng, X.Y., Zhang, B.L., Li, Z.C., Kuang, Z.K., Su, Z.D.
Revision History (Full details and data files)
- Version 1.0: 2021-06-09
Type: Initial release - Version 1.1: 2023-11-29
Changes: Data collection, Database references, Derived calculations, Refinement description
