3L46

Crystal structure of the second BRCT domain of epithelial cell transforming 2 (ECT2)

PDB DOI: https://doi.org/10.2210/pdb3L46/pdb

Classification: SIGNALING PROTEIN
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2009-12-18 Released: 2010-01-12
Deposition Author(s): Nedyalkova, L., Tempel, W., Tong, Y., Crombet, L., Wang, H., Guan, X., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Weigelt, J., Bochkarev, A., Park, H., Structural Genomics Consortium (SGC)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.48 Å
R-Value Free: 0.205
R-Value Work: 0.181
R-Value Observed: 0.182

wwPDB Validation 3D Report Full Report

This is version 1.5 of the entry. See complete history.

Literature

Crystal structure of the second BRCT domain of epithelial cell transforming 2 (ECT2)

Nedyalkova, L., Tempel, W., Tong, Y., Crombet, L., Wang, H., Guan, X., Arrowsmith, C.H., Edwards, A.M., Bountra, C., Weigelt, J., Bochkarev, A., Park, H.

To be published.

Macromolecule Content

Total Structure Weight: 26.28 kDa
Atom Count: 1,617
Modelled Residue Count: 185
Deposited Residue Count: 224
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Protein ECT2	A, B	112	Homo sapiens	Mutation(s): 0 Gene Names: ECT2
UniProt & NIH Common Fund Data Resources
Find proteins for Q9H8V3 (Homo sapiens) Explore Q9H8V3 Go to UniProtKB: Q9H8V3
PHAROS: Q9H8V3 GTEx: ENSG00000114346
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q9H8V3
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
UNX Query on UNX Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth B] SDF format, chain E [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth B] MOL2 format, chain E [auth B]	C [auth A], D [auth B], E [auth B]	UNKNOWN ATOM OR ION X		Interactions Focus chain C [auth A] Focus chain D [auth B] Focus chain E [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth B] Focus chain E [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.48 Å
R-Value Free: 0.205
R-Value Work: 0.181
R-Value Observed: 0.182
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 42.158	α = 90
b = 60.63	β = 90
c = 74.004	γ = 90

Software Package:

Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
HKL-3000	data reduction
HKL-3000	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2010-01-12

Deposition Author(s):

Structural Genomics Consortium (SGC)

Revision History (Full details and data files)

Version 1.0: 2010-01-12
Type: Initial release
Version 1.1: 2011-07-13
Changes: Version format compliance
Version 1.2: 2014-12-17
Changes: Data collection, Version format compliance
Version 1.3: 2016-10-26
Changes: Other
Version 1.4: 2017-11-01
Changes: Refinement description
Version 1.5: 2023-09-06
Changes: Data collection, Database references, Refinement description

Prepare Data

Validate Data

Deposit Data

Help and Resources

3L46

Crystal structure of the second BRCT domain of epithelial cell transforming 2 (ECT2)

Crystal structure of the second BRCT domain of epithelial cell transforming 2 (ECT2)

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)