1RBP

CRYSTALLOGRAPHIC REFINEMENT OF HUMAN SERUM RETINOL BINDING PROTEIN AT 2 ANGSTROMS RESOLUTION

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.181 

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This is version 1.4 of the entry. See complete history. 


Literature

Crystallographic refinement of human serum retinol binding protein at 2A resolution.

Cowan, S.W., Newcomer, M.E., Jones, T.A.

(1990) Proteins 8: 44-61

  • DOI: https://doi.org/10.1002/prot.340080108
  • Primary Citation of Related Structures:  
    1RBP

  • PubMed Abstract: 

    Human serum retinol binding protein (RBP) in complex with retinol has been crystallographically refined to an R-factor of 18.1% with 2A resolution data. The protein topology results in an anti-parallel beta-barrel that encapsulates the retinol ligand. A detailed description of the protein and the binding site is provided. Our structural work has helped to define a family of proteins, many of which are carrier proteins for smaller ligand molecules. We describe the structural basis for the conservation of sequence within the family.

    • Organizational Affiliation: 

    Department of Molecular Biology, Biomedicum Centre, Uppsala, Sweden.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PLASMA RETINOL-BINDING PROTEIN PRECURSOR182Homo sapiensMutation(s): 0 
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for P02753 (Homo sapiens)
Explore P02753 
Go to UniProtKB:  P02753
PHAROS:  P02753
GTEx:  ENSG00000138207 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP02753
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
RTL
Query on RTL
Download Ideal Coordinates CCD File 
B [auth A]RETINOL
C20 H30 O
FPIPGXGPPPQFEQ-OVSJKPMPSA-N
Binding Affinity Annotations 
IDSourceBinding Affinity
RTL PDBBind:  1RBP Kd: 190 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Work: 0.181 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 45.7α = 90
b = 48.7β = 90
c = 76.5γ = 90
Software Package:
Software NamePurpose
X-PLORrefinement

Structure Validation

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View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1991-07-15
    Type: Initial release
  • Version 1.1: 2008-03-03
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-11-29
    Changes: Derived calculations, Other
  • Version 1.4: 2024-11-06
    Changes: Data collection, Database references, Derived calculations, Structure summary