1LMK

THE STRUCTURE OF A BIVALENT DIABODY

PDB DOI: https://doi.org/10.2210/pdb1LMK/pdb

Classification: IMMUNOGLOBULIN
Organism(s): Mus musculus
Expression System: Escherichia coli
Mutation(s): No

Deposited: 1994-08-29 Released: 1995-03-31
Deposition Author(s): Williams, R.L.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.60 Å
R-Value Work: 0.200
R-Value Observed: 0.200

wwPDB Validation 3D Report Full Report

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

Literature

Crystal structure of a diabody, a bivalent antibody fragment.

Perisic, O., Webb, P.A., Holliger, P., Winter, G., Williams, R.L.

(1994) Structure 2: 1217-1226

PubMed: 7704531 Search on PubMed
DOI: https://doi.org/10.1016/s0969-2126(94)00123-5
Primary Citation of Related Structures:
1LMK

PubMed Abstract:
Diabodies are dimeric antibody fragments. In each polypeptide, a heavy-chain variable domain (VH) is linked to a light-chain variable domain (VL) but unlike single-chain Fv fragments, each antigen-binding site is formed by pairing of one VH and one VL domain from the two different polypeptides. Diabodies thus have two antigen-binding sites, and can be bispecific. Direct structural evidence is lacking for the connections and dimeric interactions between the two polypeptides of the diabody.

Organizational Affiliation

Centre for Protein Engineering, MRC Centre, Cambridge, UK.

Macromolecule Content

Total Structure Weight: 104.31 kDa
Atom Count: 7,613
Modelled Residue Count: 952
Deposited Residue Count: 952
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
ANTI-PHOSPHATIDYLINOSITOL SPECIFIC PHOSPHOLIPASE C DIABODY	A, B [auth C], C [auth E], D [auth G]	238	Mus musculus	Mutation(s): 0 Gene Names: L5MK16
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.60 Å
R-Value Work: 0.200
R-Value Observed: 0.200
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 72.14	α = 90
b = 80.71	β = 99.81
c = 88.01	γ = 90

Software Package:

Software Name	Purpose
X-PLOR	model building
X-PLOR	refinement
X-PLOR	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 1995-03-31

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 1995-03-31
Type: Initial release
Version 1.1: 2008-03-24
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.