Evidence map›Paper›PMID 27710932›Full record

ArticleActa crystallographica. Section D, Structural biology2016

Validation and correction of Zn-Cys

Wouter G Touw, Bart van Beusekom, Jochem M G Evers, Gert Vriend, Robbie P Joosten

Abstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed.

  1. Article
  2. Conformational dynamics in specialized CProtein science : a publication of the Protein Society · 2025
    Article
  3. Improving macromolecular structure refinement with metal-coordination restraints.Acta crystallographica. Section D, Structural biology · 2024
    Article
  4. A database overview of metal-coordination distances in metalloproteins.Acta crystallographica. Section D, Structural biology · 2024
    Article
  5. The CCP4 suite: integrative software for macromolecular crystallography.Acta crystallographica. Section D, Structural biology · 2023
    Article
  6. Review
  7. Article
  8. The missing link: covalent linkages in structural models.Acta crystallographica. Section D, Structural biology · 2021
    Article
  9. Modelling covalent linkages in CCP4.Acta crystallographica. Section D, Structural biology · 2021
    Article
  10. Article
  11. LAHMA: structure analysis through local annotation of homology-matched amino acids.Acta crystallographica. Section D, Structural biology · 2021
    Article
  12. Local and global analysis of macromolecular atomic displacement parameters.Acta crystallographica. Section D, Structural biology · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Homology-based hydrogen bond information improves crystallographic structures in the PDB.Protein science : a publication of the Protein Society · 2018
    Article
  17. Article
  18. CheckMyMetal: a macromolecular metal-binding validation tool.Acta crystallographica. Section D, Structural biology · 2017
    Article
  19. AceDRG: a stereochemical description generator for ligands.Acta crystallographica. Section D, Structural biology · 2017
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Wouter G TouwCentre for Molecular and Biomolecular Informatics, Radboud University Medical Center, Geert Grooteplein-Zuid 26-28, 6525 GA Nijmegen, The Netherlands.
Bart van BeusekomDepartment of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
Jochem M G EversCentre for Molecular and Biomolecular Informatics, Radboud University Medical Center, Geert Grooteplein-Zuid 26-28, 6525 GA Nijmegen, The Netherlands.
Gert VriendCentre for Molecular and Biomolecular Informatics, Radboud University Medical Center, Geert Grooteplein-Zuid 26-28, 6525 GA Nijmegen, The Netherlands.
Robbie P JoostenDepartment of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many crystal structures in the Protein Data Bank contain zinc ions in a geometrically distorted tetrahedral complex with four Cys and/or His ligands. A method is presented to automatically validate and correct these zinc complexes. Analysis of the corrected zinc complexes shows that the average Zn-Cys distances and Cys-Zn-Cys angles are a function of the number of cysteines and histidines involved. The observed trends can be used to develop more context-sensitive targets for model validation and refinement.

Indexed as

Binding SitesCoordination ComplexesCrystallography, X-RayCysteineDatabases, ProteinHistidineLigandsModels, MolecularProtein ConformationProteinsZincCoordination ComplexesCysteineHistidineLigandsProteinsZincgeometric restraintsprotein zinc-binding siterefinementvalidationzinc metal-site geometry

Identifiers

PMID27710932
PMCPMC5053137

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.