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PDBsum entry 6eyc

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protein ligands metals Protein-protein interface(s) links
Nuclear protein PDB id
6eyc

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
603 a.a.
605 a.a.
641 a.a.
633 a.a.
616 a.a.
689 a.a.
Ligands
ADP ×6
Metals
_ZN ×5
PDB id:
6eyc
Name: Nuclear protein
Title: Re-refinement of the mcm2-7 double hexamer using isolde
Structure: DNA replication licensing factor mcm2. Chain: 2. Synonym: minichromosome maintenance protein 2. Engineered: yes. DNA replication licensing factor mcm3. Chain: 3. Synonym: minichromosome maintenance protein 3. Engineered: yes. DNA replication licensing factor mcm4.
Source: Saccharomyces cerevisiae (strain atcc 204508 / s288c). Baker's yeast. Organism_taxid: 559292. Strain: atcc 204508 / s288c. Gene: mcm2, ybl023c, ybl0438. Expressed in: saccharomyces cerevisiae s288c. Expression_system_taxid: 559292. Gene: mcm3, yel032w, sygp-orf23.
Authors: T.I.Croll
Key ref: T.I.Croll (2018). ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps. Acta Crystallogr D Struct Biol, 74, 519-530. PubMed id: 29872003 DOI: 10.1107/S2059798318002425
Date:
11-Nov-17     Release date:   20-Jun-18    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P29469  (MCM2_YEAST) -  DNA replication licensing factor MCM2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
868 a.a.
603 a.a.
Protein chain
Pfam   ArchSchema ?
P24279  (MCM3_YEAST) -  DNA replication licensing factor MCM3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
971 a.a.
605 a.a.
Protein chain
Pfam   ArchSchema ?
P30665  (MCM4_YEAST) -  DNA replication licensing factor MCM4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
933 a.a.
641 a.a.
Protein chain
Pfam   ArchSchema ?
P29496  (MCM5_YEAST) -  Minichromosome maintenance protein 5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
775 a.a.
633 a.a.
Protein chain
Pfam   ArchSchema ?
P53091  (MCM6_YEAST) -  DNA replication licensing factor MCM6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
1017 a.a.
616 a.a.
Protein chain
Pfam   ArchSchema ?
P38132  (MCM7_YEAST) -  DNA replication licensing factor MCM7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Seq:
Struc:
 
Seq:
Struc:
845 a.a.
689 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: Chains 2, 3, 4, 5, 6, 7: E.C.3.6.4.12  - Dna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
=
ADP
Bound ligand (Het Group name = ADP)
corresponds exactly
+ phosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1107/S2059798318002425 Acta Crystallogr D Struct Biol 74:519-530 (2018)
PubMed id: 29872003  
 
 
ISOLDE: a physically realistic environment for model building into low-resolution electron-density maps.
T.I.Croll.
 
  ABSTRACT  
 
This paper introduces ISOLDE, a new software package designed to provide an intuitive environment for high-fidelity interactive remodelling/refinement of macromolecular models into electron-density maps. ISOLDE combines interactive molecular-dynamics flexible fitting with modern molecular-graphics visualization and established structural biology libraries to provide an immersive interface wherein the model constantly acts to maintain physically realistic conformations as the user interacts with it by directly tugging atoms with a mouse or haptic interface or applying/removing restraints. In addition, common validation tasks are accelerated and visualized in real time. Using the recently described 3.8 Å resolution cryo-EM structure of the eukaryotic minichromosome maintenance (MCM) helicase complex as a case study, it is demonstrated how ISOLDE can be used alongside other modern refinement tools to avoid common pitfalls of low-resolution modelling and improve the quality of the final model. A detailed analysis of changes between the initial and final model provides a somewhat sobering insight into the dangers of relying on a small number of validation metrics to judge the quality of a low-resolution model.
 

 

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