5ODS

Structure of a phosphoprotein-protein complex

PDB DOI: https://doi.org/10.2210/pdb5ODS/pdb

Classification: CELL CYCLE
Organism(s): Mus musculus, Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2017-07-06 Released: 2018-03-14
Deposition Author(s): Mukherjee, M., Bayliss, R.
Funding Organization(s): Biotechnology and Biological Sciences Research Council

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 3.09 Å
R-Value Free: 0.269
R-Value Work: 0.221
R-Value Observed: 0.223

wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Structure of a phosphoprotein-protein complex

Mukherjee, M., Bayliss, R.

(2018) EMBO J

Macromolecule Content

Total Structure Weight: 266.36 kDa
Atom Count: 18,224
Modelled Residue Count: 2,336
Deposited Residue Count: 2,368
Unique protein chains: 2

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Clathrin heavy chain 1	A, B, C, D	574	Mus musculus	Mutation(s): 0 Gene Names: Cltc
UniProt
Find proteins for Q68FD5 (Mus musculus) Explore Q68FD5 Go to UniProtKB: Q68FD5
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q68FD5
Sequence Annotations Expand
Reference Sequence

Find similar proteins by: Sequence | 3D Structure

Entity ID: 2
Molecule	Chains	Sequence Length	Organism	Details	Image
LYS-GLU-SER-ALA-LEU-ARG-LYS-GLN-SEP-LEU-TYR-LEU-LYS-PHE-ASP-PRO-LEU-LEU	E, F, G, H	18	Homo sapiens	Mutation(s): 0
UniProt & NIH Common Fund Data Resources
Find proteins for Q9Y6A5 (Homo sapiens) Explore Q9Y6A5 Go to UniProtKB: Q9Y6A5
PHAROS: Q9Y6A5 GTEx: ENSG00000013810
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9Y6A5
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
SEP Query on SEP	E, F, G, H	L-PEPTIDE LINKING	C₃ H₈ N O₆ P		SER

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 3.09 Å
R-Value Free: 0.269
R-Value Work: 0.221
R-Value Observed: 0.223
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 115.52	α = 90
b = 120.04	β = 95.72
c = 123.13	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
xia2	data reduction
xia2	data scaling
PHENIX	phasing

Structure Validation

View Full Validation Report

Entry History & Funding Information

Deposition Data

Released Date: 2018-03-14

Deposition Author(s):

Funding Organization	Location	Grant Number
Biotechnology and Biological Sciences Research Council	United Kingdom	BB/L023113/1

Revision History (Full details and data files)

Version 1.0: 2018-03-14
Type: Initial release
Version 1.1: 2024-01-17
Changes: Data collection, Database references, Refinement description

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.