1CT8

CATALYTIC ANTIBODY 7C8 COMPLEX

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.211 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history. 


Literature

Diverse structural solutions to catalysis in a family of antibodies.

Gigant, B., Tsumuraya, T., Fujii, I., Knossow, M.

(1999) Structure 7: 1385-1393

  • DOI: https://doi.org/10.1016/s0969-2126(00)80028-3
  • Primary Citation of Related Structures:  
    1CT8

  • PubMed Abstract: 

    Small organic molecules coupled to a carrier protein elicit an antibody response on immunisation. The diversity of this response has been found to be very narrow in several cases. Some antibodies also catalyse chemical reactions. Such catalytic antibodies are usually identified among those that bind tightly to an analogue of the transition state (TSA) of the relevant reaction; therefore, catalytic antibodies are also thought to have restricted diversity. To further characterise this diversity, we investigated the structure and biochemistry of the catalytic antibody 7C8, one of the most efficient of those which enhance the hydrolysis of chloramphenicol esters, and compared it to the other catalytic antibodies elicited in the same immunisation.

    • Organizational Affiliation: 

    CNRS UPR 9063, Bat. 34 CNRS, Laboratoire d'Enzymologie et Biochimie Structurales, Gif-sur-Yvette Cedex, 91198, France.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
7C8 FAB FRAGMENT; SHORT CHAIN
A, C
214Mus musculusMutation(s): 0 
UniProt
Find proteins for P01837 (Mus musculus)
Explore P01837 
Go to UniProtKB:  P01837
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01837
Sequence Annotations
Expand
  • Reference Sequence
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
7C8 FAB FRAGMENT; LONG CHAIN
B, D
220Mus musculusMutation(s): 0 
UniProt
Find proteins for P01868 (Mus musculus)
Explore P01868 
Go to UniProtKB:  P01868
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP01868
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
TAA
Query on TAA
Download Ideal Coordinates CCD File 
F [auth B],
H [auth D]		[4-(2,2,2-TRIFLUORO-ACETYLAMINO)-BENZYL]-PHOSPHONIC ACID MONO-[2-(2,2-DICHLORO-1-HYDROXY-ETHYLAMINO)-3-HYDROXY-1-(4-NITRO-PHENYL)-PROPYL] ESTER
C20 H21 Cl2 F3 N3 O8 P
PXDSVFRUDNCBRZ-NUJGCVRESA-N
SO4
Query on SO4
Download Ideal Coordinates CCD File 
E [auth A],
G [auth C]		SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Binding Affinity Annotations 
IDSourceBinding Affinity
TAA PDBBind:  1CT8 Kd: 300 (nM) from 1 assay(s)
Binding MOAD:  1CT8 Kd: 300 (nM) from 1 assay(s)
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.20 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.211 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 54.558α = 90
b = 65.612β = 95.56
c = 117.761γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
X-PLORrefinement

Structure Validation

View Full Validation Report



View more in-depth experimental data
Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1999-11-10
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Derived calculations, Version format compliance