| Db Source | domId | Structure Class | Residues | Contact String | Molecule | Source |
|---|---|---|---|---|---|---|
| ASTRAL-1.75B | d3ijta_ | d.129.3.9 | 140 | see topology | u'Uncharacterized protein' | Streptococcus mutans |
| ASTRAL-1.75B | d3ijwa_ | c.140.1.0 | 256 | see topology | u'Aminoglycoside N3-acetyltransferase' | Bacillus anthracis |
| ASTRAL-1.75B | d3ilwa_ | e.11.1.0 | 464 | see topology | u'DNA gyrase subunit A' | Mycobacterium tuberculosis |
| ASTRAL-1.75B | d3ilza_ | a.123.1.1 | 263 | see topology | u'Thyroid hormone receptor alpha' | Homo sapiens |
| ASTRAL-1.75B | d3im3a_ | a.31.1.1 | 50 | see topology | u'cAMP-dependent protein kinase type I-alpha regulatory subunit' | Bos taurus |
| ASTRAL-1.75B | d3imab_ | d.17.1.0 | 84 | see topology | u'Cysteine proteinase inhibitor' | Colocasia esculenta |
| ASTRAL-1.75B | d3imia_ | d.13.1.1 | 142 | see topology | u'Protein hit' | Bacillus anthracis |
| ASTRAL-1.75B | d3iofa_ | d.157.1.1 | 227 | see topology | u'Beta-lactamase' | Aeromonas hydrophila |
| ASTRAL-1.75B | d3ip0a_ | d.58.30.1 | 158 | see topology | u'2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase' | Escherichia coli |
| ASTRAL-1.75B | d3ip4c_ | a.137.12.1 | 92 | see topology | u'Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C' | Staphylococcus aureus |
| ASTRAL-1.75B | d3ipra_ | c.54.1.0 | 137 | see topology | u'PTS system, IIA component' | Enterococcus faecalis |
| ASTRAL-1.75B | d3iq0a_ | c.72.1.0 | 299 | see topology | u'Uncharacterized protein' | Escherichia coli |
| ASTRAL-1.75B | d3iqca_ | a.24.19.0 | 119 | see topology | u'Flagellar protein FliS' | Helicobacter pylori |
| ASTRAL-1.75B | d3iqla_ | b.34.2.0 | 66 | see topology | u'Endophilin-A1' | Rattus norvegicus |
| ASTRAL-1.75B | d3iqua_ | a.118.7.1 | 235 | see topology | u'14-3-3 protein sigma' | Homo sapiens |
| ASTRAL-1.75B | d3irba_ | b.40.4.15 | 136 | see topology | u'Uncharacterized protein' | Sulfolobus solfataricus |
| ASTRAL-1.75B | d3irua_ | c.108.1.0 | 268 | see topology | u'Phosphonoacetaldehyde hydrolase' | Oleispira antarctica |
| ASTRAL-1.75B | d3isga_ | e.3.1.1 | 248 | see topology | u'Beta-lactamase OXA-1' | Escherichia coli |
| ASTRAL-1.75B | d3ivra_ | e.23.1.0 | 394 | see topology | u'Putative long-chain-fatty-acid CoA ligase' | Rhodopseudomonas palustris |
| ASTRAL-1.75B | d3ivva_ | b.8.1.1 | 140 | see topology | u'Speckle-type POZ protein' | Homo sapiens |
Above table lists all the available domains in the ProLego database, from CATH and SCOP database. Each domain (row in the table), has the link to corresponding domain structure as well as the Topology link for detail analysis of proLeg-topologies. Table column heads can be read as following,