Download MendeleyCrystal structure of mammalian Rev7 in complex with human Rev3
Huber, F., Tropia, L., Emamzadah, S., Halazonetis, T.To be published.
6EKM
Crystal structure of mammalian Rev7 in complex with human Rev3 second binding site
- PDB DOI: https://doi.org/10.2210/pdb6EKM/pdb
- Classification: REPLICATION
- Organism(s): Mus musculus, Homo sapiens
- Expression System: Escherichia coli BL21
- Mutation(s): Yes
- Deposited: 2017-09-26 Released: 2018-10-10
- Funding Organization(s): Swiss National Science Foundation
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.76 Å
- R-Value Free: 0.258
- R-Value Work: 0.230
- R-Value Observed: 0.232
wwPDB Validation 3D Report Full Report
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 |
| Mitotic spindle assembly checkpoint protein MAD2B | 211 | Mus musculus | Mutation(s): 5 Gene Names: Mad2l2, Mad2b, Rev7 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q9D752 (Mus musculus) Explore Q9D752 Go to UniProtKB: Q9D752 | |||||
IMPC: MGI:1919140 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q9D752 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| DNA polymerase zeta catalytic subunit | 28 | Homo sapiens | Mutation(s): 0 Gene Names: REV3L, POLZ, REV3 EC: 2.7.7.7 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for O60673 (Homo sapiens) Explore O60673 Go to UniProtKB: O60673 | |||||
PHAROS: O60673 GTEx: ENSG00000009413 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | O60673 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.76 Å
- R-Value Free: 0.258
- R-Value Work: 0.230
- R-Value Observed: 0.232
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 39.2 | α = 90 |
| b = 48.64 | β = 90 |
| c = 116.81 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| iMOSFLM | data reduction |
| SCALA | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2018-10-10 Deposition Author(s): Huber, F., Tropia, L., Emamzadah, S., Halazonetis, T.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Swiss National Science Foundation | Switzerland | 160322 |
Revision History (Full details and data files)
- Version 1.0: 2018-10-10
Type: Initial release - Version 1.1: 2024-01-17
Changes: Data collection, Database references, Refinement description, Structure summary
