9GEZ | pdb_00009gez

Crystal structure of thioredoxin reductase from Cryptosporidium parvum in the "waiting" position

PDB DOI: https://doi.org/10.2210/pdb9GEZ/pdb

Classification: FLAVOPROTEIN
Organism(s): Cryptosporidium parvum
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2024-08-08 Released: 2025-05-07
Deposition Author(s): Gabriele, F., Palerma, M., Ardini, M., Bogard, J., Chen, X.M., Williams, D.L., Angelucci, F.
Funding Organization(s): National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.88 ?
R-Value Free:
0.264 (Depositor), 0.261 (DCC)
R-Value Work:
0.231 (Depositor), 0.232 (DCC)
R-Value Observed:
0.233 (Depositor)

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

Ligand Structure Quality Assessment

This is version 1.0 of the entry. See complete history.

Literature

Targeting Apicomplexan Parasites: Structural and Functional Characterization of Cryptosporidium Thioredoxin Reductase as a Novel Drug Target

Gabriele, F., Bogard, J.A., Palerma, M., Ardini, M., Byrne, M.E., Chen, X.M., Petukhov, P.A., Ippoliti, R., Angelucci, F., Williams, D.L.

(2025) Biochemistry

DOI: https://doi.org/10.1021/acs.biochem.5c00059

Macromolecule Content

Total Structure Weight: 114.17 kDa
Atom Count: 7,660
Modelled Residue Count: 991
Deposited Residue Count: 1,042
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Thioredoxin reductase	A, B	521	Cryptosporidium parvum	Mutation(s): 0 Gene Names: TRx
UniProt
Find proteins for C8CCG0 (Cryptosporidium parvum) Explore C8CCG0 Go to UniProtKB: C8CCG0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	C8CCG0
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FAD Query on FAD Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth B] MOL2 format, chain C [auth A] MOL2 format, chain D [auth B] mmCIF format, chain C [auth A] mmCIF format, chain D [auth B]	C [auth A], D [auth B]	FLAVIN-ADENINE DINUCLEOTIDE C₂₇ H₃₃ N₉ O₁₅ P₂ VWWQXMAJTJZDQX-UYBVJOGSSA-N		Interactions Focus chain C [auth A] Focus chain D [auth B] Interactions & Density Focus chain C [auth A] Focus chain D [auth B]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.88 ?
R-Value Free: 0.264 (Depositor), 0.261 (DCC)
R-Value Work: 0.231 (Depositor), 0.232 (DCC)
R-Value Observed: 0.233 (Depositor)

Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( ? )	Angle ( ? )
a = 73.553	α = 90
b = 74.177	β = 90
c = 188.574	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
XDS	data reduction
Aimless	data scaling
PHASER	phasing

Structure Validation

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Ligand Structure Quality Assessment

Entry History & Funding Information

Deposition Data

Released Date: 2025-05-07

Deposition Author(s):

Funding Organization	Location	Grant Number
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)	United States	R01AI177493

Revision History (Full details and data files)

Version 1.0: 2025-05-07
Type: Initial release

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.