3W94

Structure of Oryzias latipes enteropeptidase light chain

PDB DOI: https://doi.org/10.2210/pdb3W94/pdb

Classification: HYDROLASE
Organism(s): Oryzias latipes
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2013-03-26 Released: 2014-02-19
Deposition Author(s): Hu, S., Xu, J., Wang, H., Guo, Y.J.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.241
R-Value Work: 0.193
R-Value Observed: 0.195

wwPDB Validation 3D Report Full Report

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

Literature

Structure basis for the unique specificity of medaka enteropeptidase light chain.

Xu, J., Hu, S., Wang, X., Zhao, Z., Zhang, X., Wang, H., Zhang, D., Guo, Y.

(2014) Protein Cell 5: 178-181

PubMed: 24481630 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1007/s13238-013-0008-x
Primary Citation of Related Structures:
3W94

Organizational Affiliation

School of Pharmacy, Shanghai Jiao Tong University, Shanghai, 200240, China.

Macromolecule Content

Total Structure Weight: 52.07 kDa
Atom Count: 3,931
Modelled Residue Count: 470
Deposited Residue Count: 470
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Enteropeptidase-1	A, B	235	Oryzias latipes	Mutation(s): 0 Gene Names: EP-1
UniProt
Find proteins for A4UWM5 (Oryzias latipes) Explore A4UWM5 Go to UniProtKB: A4UWM5
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	A4UWM5
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.00 Å
R-Value Free: 0.241
R-Value Work: 0.193
R-Value Observed: 0.195
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 48.47	α = 90
b = 71.641	β = 90
c = 134.433	γ = 90

Software Package:

Software Name	Purpose
HKL-2000	data collection
PHASES	phasing
PHENIX	refinement
HKL-2000	data reduction
HKL-2000	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2014-02-19

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2014-02-19
Type: Initial release
Version 1.1: 2022-08-24
Changes: 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.