PDBsum entry 1kn4

Immune system

PDB id: 1kn4

Contents

Protein chains

219 a.a. *

222 a.a. *

Ligands

PDE

Metals

_ZN ×7

Waters ×151

* Residue conservation analysis

PDB id:

1kn4

Name:

Immune system

Title:

Catalytic antibody d2.3 complex

Structure:

Ig antibody d2.3 (light chain). Chain: l. Ig antibody d2.3 (heavy chain). Chain: h

Source:

Mus musculus. House mouse. Organism_taxid: 10090. Organism_taxid: 10090

Biol. unit:

Dimer (from PQS)

Resolution:

1.90Å R-factor: 0.213 R-free: 0.246

Authors:

B.Gigant,M.Knossow

Key ref:

L.J.D'Souza et al. (2002). Remarkable remote chiral recognition in a reaction mediated by a catalytic antibody. J Am Chem Soc, 124, 2114-2115. PubMed id: 11878955 DOI: 10.1021/ja0170504

Date:

18-Dec-01 Release date: 13-Mar-02

Protein chain

Q58EU8  (Q58EU8_MOUSE) -  Igk protein from Mus musculus

Seq: 239 a.a.

Struc: 219 a.a.*

Protein chain

P01863  (GCAA_MOUSE) -  Ig gamma-2A chain C region, A allele from Mus musculus

Seq: 330 a.a.

Struc: 222 a.a.

* PDB and UniProt seqs differ at 13 residue positions (black crosses)

DOI no: 10.1021/ja0170504

J Am Chem Soc 124:2114-2115 (2002)

PubMed id: 11878955

Remarkable remote chiral recognition in a reaction mediated by a catalytic antibody.

L.J.D'Souza, B.Gigant, M.Knossow, B.S.Green.

ABSTRACT

The crystal structures of catalytic antibody D2.3 Fab with the two enantiomers, 7D and 7L, which represent transition state analogues for the hydrolysis of the corresponding esters, 6D and 6L, were determined to better understand remarkable reactivity differences: the L-ester displayed significantly tighter binding (K(M)) and increased catalytic activity (k(cat)) with D2.3, even though the chiral center is 7 bonds distant from the reaction center. Surprisingly, the electron densities of the liganded phosphonates, 7D and 7L, within the D2.3 binding/reaction site were essentially identical, highlighting the subtle influences of protein interactions on chemical behavior.