3I35

Human SH3 domain of protein LASP1

PDB DOI: https://doi.org/10.2210/pdb3I35/pdb

Deposited: 2009-06-30 Released: 2009-09-08
Deposition Author(s): Siponen, M.I., Roos, A.K., Arrowsmith, C.H., Berglund, H., Bountra, C., Collins, R., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Johansson, A., Johansson, I., Karlberg, T., Kotenyova, T., Kotzsch, A., Kragh Nielsen, T., Moche, M., Nyman, T., Persson, C., Sagemark, J., Schueler, H., Schutz, P., Thorsell, A.G., Tresaugues, L., Van Den Berg, S., Weigelt, J., Welin, M., Wisniewska, M., Nordlund, P., Structural Genomics Consortium (SGC)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.40 Å
R-Value Free: 0.222
R-Value Work: 0.202
R-Value Observed: 0.203

wwPDB Validation 3D Report Full Report

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

Literature

Human SH3 domain of protein LASP1

Siponen, M.I., Roos, A.K., Arrowsmith, C.H., Berglund, H., Bountra, C., Collins, R., Edwards, A.M., Flodin, S., Flores, A., Graslund, S., Hammarstrom, M., Johansson, A., Johansson, I., Karlberg, T., Kotenyova, T., Kotzsch, A., Kragh Nielsen, T., Moche, M., Nyman, T., Persson, C., Sagemark, J., Schueler, H., Schutz, P., Thorsell, A.G., Tresaugues, L., Van Den Berg, S., Weigelt, J., Welin, M., Wisniewska, M., Nordlund, P.

To be published.

Macromolecule Content

Total Structure Weight: 6.62 kDa
Atom Count: 503
Modelled Residue Count: 57
Deposited Residue Count: 60
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
LIM and SH3 domain protein 1	A	60	Homo sapiens	Mutation(s): 0 Gene Names: LASP1, MLN50
UniProt & NIH Common Fund Data Resources
Find proteins for Q14847 (Homo sapiens) Explore Q14847 Go to UniProtKB: Q14847
PHAROS: Q14847 GTEx: ENSG00000002834
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q14847
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.40 Å
R-Value Free: 0.222
R-Value Work: 0.202
R-Value Observed: 0.203
Space Group: P 1 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 25.348	α = 90
b = 23.235	β = 92.47
c = 44.716	γ = 90

Software Package:

Software Name	Purpose
RAYONICS	data collection
MOLREP	phasing
REFMAC	refinement
XDS	data reduction
XSCALE	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2009-09-08

Deposition Author(s):

Structural Genomics Consortium (SGC)

Revision History (Full details and data files)

Version 1.0: 2009-09-08
Type: Initial release
Version 1.1: 2011-07-13
Changes: Refinement description, Version format compliance
Version 1.2: 2018-01-24
Changes: Database references, Structure summary
Version 1.3: 2024-02-21
Changes: Data collection, Database references

Prepare Data

Validate Data

Deposit Data

Help and Resources

3I35

Human SH3 domain of protein LASP1

Human SH3 domain of protein LASP1

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)