9QZG | pdb_00009qzg

GID4 in complex with Compound 18


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 
    0.336 (Depositor), 0.346 (DCC) 
  • R-Value Work: 
    0.276 (Depositor), 0.285 (DCC) 
  • R-Value Observed: 
    0.279 (Depositor) 

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

Validation slider image for 9QZG

This is version 1.0 of the entry. See complete history

Literature

Novel chemical probes and conformational flexibility of GID4 - a substrate receptor of the Human CTLH E3 ligase complex

Klejnot, M.Gorecka-Minakowska, K.M.Pastok, M.W.Skowron, A.N.Wisniewski, J.Walczak, M.J.

To be published.

Macromolecule Content 

  • Total Structure Weight: 20.02 kDa 
  • Atom Count: 1,380 
  • Modeled Residue Count: 159 
  • Deposited Residue Count: 166 
  • Unique protein chains: 1

Macromolecules

Find similar proteins by:|  3D Structure
Entity ID: 1
MoleculeChains  Sequence LengthOrganismDetailsImage
Glucose-induced degradation protein 4 homolog166Homo sapiensMutation(s): 0 
Gene Names: GID4C17orf39VID24
UniProt & NIH Common Fund Data Resources
Find proteins for Q8IVV7 (Homo sapiens)
Explore Q8IVV7 
Go to UniProtKB:  Q8IVV7
PHAROS:  Q8IVV7
GTEx:  ENSG00000141034 
Entity Groups
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ8IVV7
Sequence Annotations
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Reference Sequence

Small Molecules

Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
A1JCC

Query on A1JCC



Download:Ideal Coordinates CCD File
B [auth A]~{N}-[3-fluoranyl-5-[4-(4-methoxypiperidin-1-yl)carbonyl-5-methyl-furan-2-yl]phenyl]-4,4-dimethyl-piperidine-1-carboximidamide
C26 H35 F N4 O3
PYNQAYNMHITVOO-UHFFFAOYSA-N

Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free:  0.336 (Depositor), 0.346 (DCC) 
  • R-Value Work:  0.276 (Depositor), 0.285 (DCC) 
  • R-Value Observed: 0.279 (Depositor) 
Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 40.255α = 90
b = 41.752β = 90
c = 103.205γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
PDB_EXTRACTdata extraction
XDSdata reduction
XDSdata scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History 

& Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Center for Research and Development (Poland)PolandPOIR.01.01.01-00-0931/19

Revision History  (Full details and data files)

  • Version 1.0: 2026-05-06
    Type: Initial release