4L41

Human Lactose synthase: A 2:1 complex between human alpha-lactalbumin and human beta1,4-galactosyltransferase


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.190 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Crystal Structure of Human Lactose Synthase forms a Novel 1:2 Complex between beta1,4Galactosyltransferase 1 and alpha-Lactalbumin Proteins

Ramakrishnan, B.Qasba, P.K.

To be published.

Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Alpha-lactalbuminA,
C [auth B]
124Homo sapiensMutation(s): 0 
Gene Names: 4-galactosyltransferasebeta1LALBALYZL7
UniProt & NIH Common Fund Data Resources
Find proteins for P00709 (Homo sapiens)
Explore P00709 
Go to UniProtKB:  P00709
PHAROS:  P00709
GTEx:  ENSG00000167531 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP00709
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Beta-1,4-galactosyltransferase 1B [auth C]287Homo sapiensMutation(s): 2 
Gene Names: alpha-lactalbuminB4GALT1GGTB2
EC: 2.4.1.22
UniProt & NIH Common Fund Data Resources
Find proteins for P15291 (Homo sapiens)
Explore P15291 
Go to UniProtKB:  P15291
PHAROS:  P15291
GTEx:  ENSG00000086062 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP15291
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Free: 0.237 
  • R-Value Work: 0.188 
  • R-Value Observed: 0.190 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 62.39α = 90
b = 65.21β = 114.45
c = 71.72γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
PHENIXmodel building
PHENIXrefinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-10-02
    Type: Initial release
  • Version 1.1: 2023-09-20
    Changes: Data collection, Database references, Derived calculations, Refinement description