1COF

YEAST COFILIN, ORTHORHOMBIC CRYSTAL FORM

PDB DOI: https://doi.org/10.2210/pdb1COF/pdb

Classification: ACTIN-BINDING PROTEIN
Organism(s): Saccharomyces cerevisiae
Expression System: Escherichia coli
Mutation(s): No

Deposited: 1996-11-26 Released: 1997-04-01
Deposition Author(s): Fedorov, A.A., Lappalainen, P., Fedorov, E.V., Drubin, D.G., Almo, S.C.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Work: 0.184

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Structure determination of yeast cofilin.

Fedorov, A.A., Lappalainen, P., Fedorov, E.V., Drubin, D.G., Almo, S.C.

(1997) Nat Struct Biol 4: 366-369

PubMed: 9145106 Search on PubMed
DOI: https://doi.org/10.1038/nsb0597-366
Primary Citation of Related Structures:
1CFY, 1COF, 1QPV

PubMed Abstract:
Cofilin, a ubiquitous 15,000 M(r) protein, plays a central role in regulating cytoskeletal dynamics. Cofilin binds to actin monomers and filaments, and has a pH-dependent actin severing activity. The structure will allow for a detailed analysis of cofilin function.

Macromolecule Content

Total Structure Weight: 15.92 kDa
Atom Count: 1,097
Modelled Residue Count: 135
Deposited Residue Count: 143
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
COFILIN	A	143	Saccharomyces cerevisiae	Mutation(s): 0
UniProt
Find proteins for Q03048 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore Q03048 Go to UniProtKB: Q03048
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q03048
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Work: 0.184
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 30.669	α = 90
b = 48.773	β = 90
c = 101.367	γ = 90

Software Package:

Software Name	Purpose
PHASES	phasing
X-PLOR	model building
PROFFT	refinement
X-PLOR	refinement
XDS	data reduction
XSCALE	data scaling
X-PLOR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1997-04-01

Deposition Author(s):

Lappalainen, P.

Revision History (Full details and data files)

Version 1.0: 1997-04-01
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2024-02-07
Changes: Data collection, Database references

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.