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PO4 Phosphate ion
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Code : 1A2Y   PDBj   RCSB PDB   PDBe
Header : COMPLEX (IMMUNOGLOBULIN/HYDROLASE)
Title : HEN EGG WHITE LYSOZYME, D18A MUTANT, IN COMPLEX WITH MOUSE MONOCLONAL ANTIBODY D1.3
Release Data : 1998-04-29
Compound :
mol_id molecule chains
1 IGG1-KAPPA D1.3 FV (LIGHT CHAIN) A
mol_id molecule chains
2 IGG1-KAPPA D1.3 FV (HEAVY CHAIN) B
mol_id molecule chains
3 LYSOZYME C
ec: 3.2.1.17
mutation: D18A
Source :
mol_id organism_scientific organism_common expression_system
1 Mus musculus  (taxid:10090) House mouse Escherichia coli  (taxid:562)
organ: EGG
mol_id organism_scientific organism_common expression_system
2 Mus musculus  (taxid:10090) House mouse Escherichia coli  (taxid:562)
organ: EGG
mol_id organism_scientific organism_common expression_system
3 Gallus gallus  (taxid:9031) Chicken Saccharomyces cerevisiae  (taxid:4932)
organ: EGG
cell: EGG
cellular_location: CYTOPLASM (WHITE)
expression_system_common: Baker's yeast
Authors : Tsuchiya, D., Mariuzza, R.A.
Keywords : COMPLEX (IMMUNOGLOBULIN-HYDROLASE), IMMUNOGLOBULIN V REGION, HYDROLASE, GLYCOSIDASE, BACTERIOLYTIC ENZYME, EGG WHITE, COMPLEX (IMMUNOGLOBULIN-HYDROLASE) complex
Exp. method : X-RAY DIFFRACTION ( 1.5 Å )
Citation :

A mutational analysis of binding interactions in an antigen-antibody protein-protein complex.

Dall'Acqua, W.,Goldman, E.R.,Lin, W.  et al.
(1998)  Biochemistry  37 : 7981 - 7991

PubMed: 9609690
DOI: 10.1021/bi980148j

Hydrogen Bonding and Solvent Structure in an Antigen-Antibody Interface. Crystal Structures and Thermodynamic Characterization of Three Fv Mutants Complexed with Lysozyme

Fields, B.A.,Goldbaum, F.A.,Dall'Acqua, W.  et al.
(1996)  Biochemistry  35 : 15494

Bound Water Molecules and Conformational Stabilization Help Mediate an Antigen-Antibody Association

Bhat, T.N.,Bentley, G.A.,Boulot, G.  et al.
(1994)  Proc.Natl.Acad.Sci.USA  91 : 1089

Solvent Rearrangement in an Antigen-Antibody Interface Introduced by Site-Directed Mutagenesis of the Antibody Combining Site

Ysern, X.,Fields, B.A.,Bhat, T.N.  et al.
(1994)  J.Mol.Biol.  238 : 496

Chain : A
UniProt : P01635 (KV5A3_MOUSE)
Reaction : -
Chain : B
UniProt : P01820 (HVM44_MOUSE)
Reaction : -
Chain : C
UniProt : P00698 (LYSC_CHICK)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. 3.2.1.17 -
-