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SAbDab specifications


Unique identifier OMICS_03062
Name SAbDab
Alternative name Structural antibody database
Restrictions to use None
Maintained No

Publication for Structural antibody database

SAbDab citations


Repertoire Analysis of Antibody CDR H3 Loops Suggests Affinity Maturation Does Not Typically Result in Rigidification

Front Immunol
PMCID: 5840193
PMID: 29545810
DOI: 10.3389/fimmu.2018.00413

[…] e actual antibody structure. Thus, we applied FIRST-PG analysis to a large set of antibody crystal structures. We curated the set of all non-redundant mouse and human antibody crystal structures from SAbDab (). To be consistent with the models produced by RosettaAntibody, we truncated the structure of each antibody to only the Fv domain, excluding other antibody regions or antigen. Then, we used I […]


Antibody H3 Structure Prediction

Comput Struct Biotechnol J
PMCID: 5312500
PMID: 28228926
DOI: 10.1016/j.csbj.2017.01.010

[…] Sphinx is a recently-developed method that integrates knowledge-based and ab initio approachesĀ . An H3-specific version is freely available for use at The algorithm starts with a database search; loop fragments that are shorter than the target loop are extracted based on their sequence similarity to the target. The struc […]


Examining Variable Domain Orientations in Antigen Receptors Gives Insight into TCR Like Antibody Design

PLoS Comput Biol
PMCID: 4168974
PMID: 25233457
DOI: 10.1371/journal.pcbi.1003852

[…] The orientations of each of the TCR-like antibodies found in SAbDab were calculated using the ABangle methodology. Supplementary Figure S2 in shows where each of these lie compared to the background antibody distribution. There appears to be no preference for […]


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SAbDab institution(s)
Department of Statistics, University of Oxford, Oxford, UK; Informatics, UCB Pharma, Slough, UK; Roche Pharma Research and Early Development, Chinahe Diagnostics GmbH, Penzberg, Germany

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