2EHO

Crystal structure of human GINS complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.274 
  • R-Value Work: 0.221 
  • R-Value Observed: 0.221 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Crystal structure of the human GINS complex

Choi, J.M.Lim, H.S.Kim, J.J.Song, O.K.Cho, Y.

(2007) Genes Dev 21: 1316-1321

  • DOI: https://doi.org/10.1101/gad.1548107
  • Primary Citation of Related Structures:  
    2EHO

  • PubMed Abstract: 

    The GINS complex mediates the assembly of the MCM2-7 (minichromosome maintenance) complex with proteins in a replisome progression complex. The eukaryotic GINS complex is composed of Sld5, Psf1, Psf2, and Psf3, which must be assembled for cell proliferation. We determined the crystal structure of the human GINS complex: GINS forms an elliptical shape with a small central channel. The structures of Sld5 and Psf2 resemble those of Psf1 and Psf3, respectively. In addition, the N-terminal and C-terminal domains of Sld5/Psf1 are permuted in Psf2/Psf3, which suggests that the four proteins have evolved from a common ancestor. Using a structure-based mutational analysis, we identified the functionally critical surface regions of the GINS complex.


  • Organizational Affiliation

    National Creative Initiatives for Structural Biology, Pohang University of Science and Technology, Pohang, Kyung Book 790-784, South Korea.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
GINS complex subunit 4
A, E, I
203Homo sapiensMutation(s): 8 
UniProt & NIH Common Fund Data Resources
Find proteins for Q9BRT9 (Homo sapiens)
Explore Q9BRT9 
Go to UniProtKB:  Q9BRT9
PHAROS:  Q9BRT9
GTEx:  ENSG00000147536 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9BRT9
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
DNA replication complex GINS protein PSF1
B, F, J
152Homo sapiensMutation(s): 7 
Gene Names: Psf1
UniProt & NIH Common Fund Data Resources
Find proteins for Q14691 (Homo sapiens)
Explore Q14691 
Go to UniProtKB:  Q14691
PHAROS:  Q14691
GTEx:  ENSG00000101003 
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UniProt GroupQ14691
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
DNA replication complex GINS protein PSF2
C, G, K
186Homo sapiensMutation(s): 8 
Gene Names: PSF2
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Find proteins for Q9Y248 (Homo sapiens)
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Go to UniProtKB:  Q9Y248
PHAROS:  Q9Y248
GTEx:  ENSG00000131153 
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UniProt GroupQ9Y248
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
GINS complex subunit 3
D, H, L
216Homo sapiensMutation(s): 6 
Gene Names: Psf3
UniProt & NIH Common Fund Data Resources
Find proteins for Q9BRX5 (Homo sapiens)
Explore Q9BRX5 
Go to UniProtKB:  Q9BRX5
PHAROS:  Q9BRX5
GTEx:  ENSG00000181938 
Entity Groups  
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UniProt GroupQ9BRX5
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  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
SO4
Query on SO4

Download Ideal Coordinates CCD File 
AA [auth K]
BA [auth L]
CA [auth L]
M [auth A]
N [auth B]
AA [auth K],
BA [auth L],
CA [auth L],
M [auth A],
N [auth B],
O [auth E],
P [auth E],
Q [auth E],
R [auth E],
S [auth F],
T [auth F],
U [auth F],
V [auth F],
W [auth I],
X [auth I],
Y [auth I],
Z [auth J]
SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
MSE
Query on MSE
A, E, I
L-PEPTIDE LINKINGC5 H11 N O2 SeMET
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.00 Å
  • R-Value Free: 0.274 
  • R-Value Work: 0.221 
  • R-Value Observed: 0.221 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 164.935α = 90
b = 176.995β = 105.91
c = 126.508γ = 90
Software Package:
Software NamePurpose
CNSrefinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
CNSphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2007-06-19
    Type: Initial release
  • Version 1.1: 2008-04-30
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance