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Database Profile

multidom

General information

URL: http://prodata.swmed.edu/multidom/
Full name: A database of domain definitions for proteins with complex interdomain geometry
Description: Defining structural domains for some multi-domain proteins is difficult. These examples have been grouped under "Multi-domain proteins" by SCOP and described as "Folds consisting of two or more domains belonging to different classes". Representative PDB chains were selected from this "Multi-domain class".
Year founded: 2009
Last update: 2008-11
Version:
Accessibility:
Accessible
Country/Region: United States

Classification & Tag

Data type:
Data object:
NA
Database category:
Major species:
NA
Keywords:

Contact information

University/Institution: University of Texas Southwestern Medical Center
Address:
City: Dallas
Province/State: Texas
Country/Region: United States
Contact name (PI/Team): Nick V. Grishin
Contact email (PI/Helpdesk): grishin@chop.swmed.edu

Publications

19352501
A database of domain definitions for proteins with complex interdomain geometry. [PMID: 19352501]
Majumdar I, Kinch LN, Grishin NV.

Protein structural domains are necessary for understanding evolution and protein folding, and may vary widely from functional and sequence based domains. Although, various structural domain databases exist, defining domains for some proteins is non-trivial, and definitions of their domain boundaries are not available. Here, we present a novel database of manually defined structural domains for a representative set of proteins from the SCOP "multi-domain proteins" class. (http://prodata.swmed.edu/multidom/). We consider our domains as mobile evolutionary units, which may rearrange during protein evolution. Additionally, they may be visualized as structurally compact and possibly independently folding units. We also found that representing domains as evolutionary and folding units do not always lead to a unique domain definition. However, unlike existing databases, we retain and refine these "alternate" domain definitions after careful inspection of structural similarity, functional sites and automated domain definition methods. We provide domain definitions, including actual residue boundaries, for proteins that well known databases like SCOP and CATH do not attempt to split. Our alternate domain definitions are suitable for sequence and structure searches by automated methods. Additionally, the database can be used for training and testing domain delineation algorithms. Since our domains represent structurally compact evolutionary units, the database may be useful for studying domain properties and evolution.

PLoS One. 2009:4(4) | 16 Citations (from Europe PMC, 2025-12-13)

Ranking

All databases:
5463/6895 (20.783%)
Structure:
747/967 (22.854%)
Modification:
304/337 (10.089%)
5463
Total Rank
15
Citations
0.938
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Record metadata

Created on: 2018-01-26
Curated by:
Lin Liu [2022-09-20]
Zhuang Xiong [2018-02-24]