![]() | Class c: Alpha and beta proteins (a/b) [51349] (148 folds) |
![]() | Fold c.1: TIM beta/alpha-barrel [51350] (33 superfamilies) contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678 the first seven superfamilies have similar phosphate-binding sites |
![]() | Superfamily c.1.12: Phosphoenolpyruvate/pyruvate domain [51621] (8 families) ![]() |
![]() | Family c.1.12.8: Ketopantoate hydroxymethyltransferase PanB [89503] (2 proteins) automatically mapped to Pfam PF02548 |
![]() | Protein Ketopantoate hydroxymethyltransferase PanB [89504] (3 species) dodecameric enzyme; a C-terminal helix exchange is observed in the M. tuberculosis enzyme but not in the E. coli enzyme |
![]() | Species Neisseria meningitidis [TaxId:487] [102100] (2 PDB entries) |
![]() | Domain d1o66c1: 1o66 C:2-256 [92549] Other proteins in same PDB: d1o66a2, d1o66b2, d1o66c2, d1o66d2, d1o66e2 structural genomics complexed with gol |
PDB Entry: 1o66 (more details), 1.75 Å
SCOPe Domain Sequences for d1o66c1:
Sequence, based on SEQRES records: (download)
>d1o66c1 c.1.12.8 (C:2-256) Ketopantoate hydroxymethyltransferase PanB {Neisseria meningitidis [TaxId: 487]} itvntlqkmkaagekiamltayessfaalmddagvemllvgdslgmavqgrkstlpvslr dmcyhtecvargaknamivsdlpfgayqqskeqafaaaaelmaagahmvkleggvwmaet teflqmrgipvcahigltpqsvfafggykvqgrggkaqallndakahddagaavvlmecv laelakkvtetvscptigigagadcdgqvlvmhdmlgifpgktakfvknfmqghdsvqaa vrayvaevkaktfpa
>d1o66c1 c.1.12.8 (C:2-256) Ketopantoate hydroxymethyltransferase PanB {Neisseria meningitidis [TaxId: 487]} itvntlqkmkaagekiamltayessfaalmddagvemllvgdslgmavqgrkstlpvslr dmcyhtecvargaknamivsdlpfgayqqskeqafaaaaelmaagahmvkleggvwmaet teflqmrgipvcahigltpqsvfakaqallndakahddagaavvlmecvlaelakkvtet vscptigigagadcdgqvlvmhdmlgifpgktakfvknfmqghdsvqaavrayvaevkak tfpa
Timeline for d1o66c1: