| Db Source | domId | Structure Class | Residues | Contact String | Molecule | Source |
|---|---|---|---|---|---|---|
| ASTRAL-1.75B | d1avwb_ | b.42.4.1 | 171 | see topology | u'Trypsin inhibitor A' | Glycine max |
| ASTRAL-1.75B | d1aw9a1 | a.45.1.1 | 135 | see topology | u'Glutathione transferase III(A)' | Zea mays |
| ASTRAL-1.75B | d1awcb_ | d.211.1.1 | 153 | see topology | u'GA-binding protein subunit beta-1' | Mus musculus |
| ASTRAL-1.75B | d1ax8a_ | a.26.1.1 | 130 | see topology | u'Leptin' | Homo sapiens |
| ASTRAL-1.75B | d1axib1 | b.1.2.1 | 85 | see topology | u'Growth hormone receptor' | Homo sapiens |
| ASTRAL-1.75B | d1axib2 | b.1.2.1 | 106 | see topology | u'Growth hormone receptor' | Homo sapiens |
| ASTRAL-1.75B | d1ay2a_ | d.24.1.1 | 157 | see topology | u'Fimbrial protein' | Neisseria gonorrhoeae |
| ASTRAL-1.75B | d1ayaa_ | d.93.1.1 | 101 | see topology | u'Tyrosine-protein phosphatase non-receptor type 11' | Mus musculus |
| ASTRAL-1.75B | d1ayea2 | d.58.3.1 | 92 | see topology | u'Carboxypeptidase A2' | Homo sapiens |
| ASTRAL-1.75B | d1ayja_ | g.3.7.5 | 50 | see topology | u'Defensin-like protein 1' | Raphanus sativus |
| ASTRAL-1.75B | d1aym.1 | b.121.4.1 | 259 | see topology | — | — |
| ASTRAL-1.75B | d1aym1_ | b.121.4.1 | 285 | see topology | u'Genome polyprotein' | Human rhinovirus sp. |
| ASTRAL-1.75B | d1aym3_ | b.121.4.1 | 238 | see topology | u'Genome polyprotein' | Human rhinovirus sp. |
| ASTRAL-1.75B | d1ayoa_ | b.2.4.1 | 130 | see topology | u'Alpha-2-macroglobulin' | Bos taurus |
| ASTRAL-1.75B | d1azoa_ | c.52.1.14 | 212 | see topology | u'DNA mismatch repair protein MutH' | Escherichia coli |
| ASTRAL-1.75B | d1azsa_ | d.58.29.1 | 190 | see topology | u'Adenylate cyclase type 5' | Canis lupus |
| ASTRAL-1.75B | d1azsc1 | a.66.1.1 | 116 | see topology | u'Guanine nucleotide-binding protein G(s) subunit alpha isoforms short' | Bos taurus |
| ASTRAL-1.75B | d1azza_ | b.47.1.2 | 222 | see topology | u'Brachyurin' | Leptuca pugilator |
| ASTRAL-1.75B | d1b0aa2 | c.58.1.2 | 121 | see topology | u'Bifunctional protein FolD' | Escherichia coli |
| ASTRAL-1.75B | d1b0ba_ | a.1.1.2 | 141 | see topology | u'Hemoglobin-1' | Phacoides pectinatus |
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,