Structural Classification of Proteins
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Superfamily: MTH889-like

assembles into hexameric ring-like structures with the formation of a singe beta-barrel sheet of 24 strands

Lineage:

  1. Root: scop
  2. Class: Alpha and beta proteins (a+b) [53931]
    Mainly antiparallel beta sheets (segregated alpha and beta regions)
  3. Fold: Ferredoxin-like [54861]
    alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2
  4. Superfamily: MTH889-like [160363]
    assembles into hexameric ring-like structures with the formation of a singe beta-barrel sheet of 24 strands

Families:

  1. MTH889-like [160364] (2)
    Pfam 02680; DUF211, COG1888
    1. Uncharacterized protein MTH889 [160365]
      1. Methanobacterium thermoautotrophicum [TaxId: 145262] [160366] (7)
        SQ O26975 3-95
        1. 2raq picpic
          complexed with ca
          1. region a:3-95 [151827] picpiclink
        2. 2raq picpic
          automatically matched to 2RAQ A:3-95
          complexed with ca
          1. region b:3-95 [151828] picpiclink
        3. 2raq picpic
          automatically matched to 2RAQ A:3-95
          complexed with ca
          1. region c:3-95 [151829] picpiclink
        4. 2raq picpic
          automatically matched to 2RAQ A:3-95
          complexed with ca
          1. region d:3-95 [151830] picpiclink
        5. 2raq picpic
          automatically matched to 2RAQ A:3-95
          complexed with ca
          1. region e:3-95 [151831] picpiclink
        6. 2raq picpic
          automatically matched to 2RAQ A:3-95
          complexed with ca
          1. region f:3-95 [151832] picpiclink
        7. 2raq picpic
          automatically matched to 2RAQ A:3-95
          complexed with ca
          1. region g:3-95 [151833] picpiclink
    2. Uncharacterized protein AF1549 [160367]
      1. Archaeoglobus fulgidus [TaxId: 2234] [160368] (14)
        SQ O28723 1-91
        1. 3bpd picpic
          complexed with mg; mutant
          1. region a:1-91 [155471] picpiclink
        2. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region b:1-90 [155472] picpiclink
        3. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region c:1-90 [155473] picpiclink
        4. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region d:1-91 [155474] picpiclink
        5. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region e:1-90 [155475] picpiclink
        6. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region f:1-91 [155476] picpiclink
        7. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region g:1-90 [155477] picpiclink
        8. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region h:1-90 [155478] picpiclink
        9. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region i:1-90 [155479] picpiclink
        10. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region j:1-90 [155480] picpiclink
        11. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region k:1-91 [155481] picpiclink
        12. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region l:1-90 [155482] picpiclink
        13. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region m:1-90 [155483] picpiclink
        14. 3bpd picpic
          automatically matched to 3BPD A:1-91
          complexed with mg; mutant
          1. region n:1-90 [155484] picpiclink

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MRC
site Generated from scop database 1.75 with scopm 1.101 on Wed Jun 3 10:42:06 2009
Copyright © 1994-2009 The scop authors / scop@mrc-lmb.cam.ac.uk