1VJ1

Crystal structure of putative NADPH-dependent oxidoreductase from Mus musculus at 2.10 A resolution

PDB DOI: https://doi.org/10.2210/pdb1VJ1/pdb

Classification: UNKNOWN FUNCTION
Organism(s): Mus musculus
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2003-12-03 Released: 2003-12-09
Deposition Author(s): Joint Center for Structural Genomics (JCSG)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free: 0.216
R-Value Work: 0.180
R-Value Observed: 0.182

wwPDB Validation 3D Report Full Report

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

Literature

Crystal structure of a putative NADPH-dependent oxidoreductase (GI: 18204011) from mouse at 2.10 A resolution

Levin, I., Schwarzenbacher, R., McMullan, D., Abdubek, P., Ambing, E., Biorac, T., Cambell, J., Canaves, J.M., Chiu, H.J., Dai, X., Deacon, A.M., DiDonato, M., Elsliger, M.A., Godzik, A., Grittini, C., Grzechnik, S.K., Hampton, E., Jaroszewski, L., Karlak, C., Klock, H.E., Koesema, E., Kreusch, A., Kuhn, P., Lesley, S.A., McPhillips, T.M., Miller, M.D., Morse, A., Moy, K., Ouyang, J., Page, R., Quijano, K., Reyes, R., Robb, A., Sims, E., Spraggon, G., Stevens, R.C., van den Bedem, H., Velasquez, J., Vincent, J., von Delft, F., Wang, X., West, B., Wolf, G., Xu, Q., Hodgson, K.O., Wooley, J., Wilson, I.A.

(2004) Proteins 56: 629-633

PubMed: 15229897 Search on PubMed
DOI: https://doi.org/10.1002/prot.20163
Primary Citation of Related Structures:
1VJ1

Organizational Affiliation

The Joint Center for Structural Genomics, Stanford University, Menlo Park, California, USA.

Macromolecule Content

Total Structure Weight: 39.97 kDa
Atom Count: 2,720
Modelled Residue Count: 341
Deposited Residue Count: 363
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
putative NADPH-dependent oxidoreductase	A	363	Mus musculus	Mutation(s): 9 Gene Names: ZADH1
UniProt
Find proteins for Q8VDQ1 (Mus musculus) Explore Q8VDQ1 Go to UniProtKB: Q8VDQ1
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q8VDQ1
Sequence Annotations Expand
Reference Sequence

Small Molecules

Modified Residues 1 Unique
ID	Chains	Type	Formula	2D Diagram	Parent
MSE Query on MSE	A	L-PEPTIDE LINKING	C₅ H₁₁ N O₂ Se		MET

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free: 0.216
R-Value Work: 0.180
R-Value Observed: 0.182
Space Group: P 2₁ 2₁ 2₁
Diffraction Data: https://doi.org/10.18430/M31VJ1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 42.386	α = 90
b = 91.805	β = 90
c = 100.565	γ = 90

Software Package:

Software Name	Purpose
MOSFLM	data reduction
SCALA	data scaling
SOLVE	phasing
RESOLVE	model building
REFMAC	refinement
CCP4	data scaling
RESOLVE	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2003-12-09

Deposition Author(s):

Joint Center for Structural Genomics (JCSG)

Revision History (Full details and data files)

Version 1.0: 2003-12-09
Type: Initial release
Version 1.1: 2008-04-26
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Advisory, Version format compliance
Version 1.3: 2023-01-25
Changes: Database references, Derived calculations

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.