1MCP

PHOSPHOCHOLINE BINDING IMMUNOGLOBULIN FAB MC/PC603. AN X-RAY DIFFRACTION STUDY AT 2.7 ANGSTROMS


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Work: 0.225 

wwPDB Validation   3D Report Full Report


This is version 2.0 of the entry. See complete history


Literature

Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A.

Satow, Y.Cohen, G.H.Padlan, E.A.Davies, D.R.

(1986) J Mol Biol 190: 593-604

  • DOI: https://doi.org/10.1016/0022-2836(86)90245-7
  • Primary Citation of Related Structures:  
    1MCP

  • PubMed Abstract: 

    The crystal structure of the Fab of McPC603, a phosphocholine-binding mouse myeloma protein, has been refined at 2.7 A resolution by a combination of restrained least-squares refinement and molecular modeling. The overall structure remains as previously reported, with an elbow bend angle between the variable and constant modules of 133 degrees. Some adjustments have been made in the structure of the loops as a result of the refinement. The hypervariable loops are all visible in the electron density map with the exception of three residues in the first hypervariable loop of the light chain. A sulfate ion occupies the site of binding of the phosphate moiety of phosphocholine.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
IGA-KAPPA MCPC603 FAB (LIGHT CHAIN)A [auth L]220Mus musculusMutation(s): 0 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
IGA-KAPPA MCPC603 FAB (HEAVY CHAIN)B [auth H]222Mus musculusMutation(s): 0 
UniProt
Find proteins for P01789 (Mus musculus)
Explore P01789 
Go to UniProtKB:  P01789
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01789
Sequence Annotations
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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 
C [auth H]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.70 Å
  • R-Value Work: 0.225 
  • Space Group: P 63
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 162.531α = 90
b = 162.531β = 90
c = 60.719γ = 120

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1985-01-02
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Advisory, Version format compliance
  • Version 2.0: 2023-07-26
    Type: Remediation
    Changes: Advisory, Atomic model, Data collection, Database references, Derived calculations, Other