Download MendeleyCrystal structure of N-terminal domain of human FACT complex subunit SSRP1
Hu, Q., Su, D., Thompson, J.R., Botuyan, M.V., Mer, G.To be published.
5UMR
Crystal structure of N-terminal domain of human FACT complex subunit SSRP1
- PDB DOI: https://doi.org/10.2210/pdb5UMR/pdb
- Classification: TRANSCRIPTION
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2017-01-29 Released: 2018-01-31
- Funding Organization(s): National Institutes of Health/National Cancer Institute (NIH/NCI), National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.188
- R-Value Work: 0.153
- R-Value Observed: 0.155
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 |
| FACT complex subunit SSRP1 | 102 | Homo sapiens | Mutation(s): 0 Gene Names: SSRP1, FACT80 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q08945 (Homo sapiens) Explore Q08945 Go to UniProtKB: Q08945 | |||||
PHAROS: Q08945 GTEx: ENSG00000149136 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q08945 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.188
- R-Value Work: 0.153
- R-Value Observed: 0.155
- Space Group: P 43
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 37.958 | α = 90 |
| b = 37.958 | β = 90 |
| c = 67.288 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2018-01-31 Deposition Author(s): Su, D., Hu, Q., Thompson, J.R., Heroux, A., Botuyan, M.V., Mer, G.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Cancer Institute (NIH/NCI) | United States | CA132878 |
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | GM116829 |
Revision History (Full details and data files)
- Version 1.0: 2018-01-31
Type: Initial release - Version 1.1: 2019-12-04
Changes: Author supporting evidence
