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Figure 7 | BMC Bioinformatics

Figure 7

From: SCOPmap: Automated assignment of protein structures to evolutionary superfamilies

Figure 7

Homologous SCOP superfamilies. a) Ribbon diagram of thiamin phosphate synthase from Bacillus subtilis (PDB: 1g69[52], chain B) from the thiamin phosphate synthase superfamily. b) Ribbon diagram of indole-3-glycerophosphate synthase from Thermotoga maritima (PDB: 1i4n[53], chain A) from the ribulose-phosphate binding barrel superfamily. c) Pairwise alignment of representatives of the thiamin phosphate synthase and the ribulose-phosphate binding barrel superfamily produced by PSI-BLAST. Residue pairs that are equivalently aligned by DaliLite are showed in red bold letters. The three phosphate-binding residues in conserved positions in these two proteins are highlighted in green in the alignment and shown in ball-and-stick format in the structure figures. d) Ribbon diagram of α subunit C-terminal domain from E. coli RNA polymerase (PDB: 1lb2[54], chain B) from the "C-terminal domain of RNA polymerase alpha subunit" superfamily. Regions of the domain involved in DNA binding are in red. e) Ribbon diagram of the N-terminal domain of Rad51 from Homo sapiens (PDB: 1b22[55], chain A) from the "DNA repair protein Rad51, N-terminal domain superfamily". Putative DNA-binding surface is in red.

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