Structural Classification of Proteins
Superfamily: beta-Roll
superhelix turns are made of two short strands each
uperfamily
Lineage:
Root:
scop
Class:
All beta proteins
[48724]
Fold:
Single-stranded right-handed beta-helix
[51125]
superhelix turns are made of parallel beta-strands and (short) turns
Superfamily:
beta-Roll
[51120]
superhelix turns are made of two short strands each
uperfamily
Families:
Serralysin-like metalloprotease, C-terminal domain
[51121] (4)
duplication: halfturs of beta-helix are sequence and structural repeats; binds calcium ions between the turns
Metalloprotease [51122]
The catalytic N-terminal domain belong to the "zincin" superfamily
Pseudomonas aeruginosa
[TaxId: 287]
[51123] (3)
alkaline protease
1kap
complexed with ca, zn
region p:247-470
[28012]
1jiw
complexed with ca, zn
region p:247-470
[63079]
1akl
complexed with ca, zn
region a:247-470
[28013]
Serratia marcescens
[TaxId: 615]
[51124] (4)
serralysin
1sat
complexed with ca, zn
region a:247-471
[28014]
1af0
complexed with ca, hma, zn
region a:247-471
[28017]
1srp
complexed with ca, zn
region a:247-471
[28015]
1smp
complexed with ca, zn
region a:247-471
[28016]
Erwinia chrysanthemi
[TaxId: 556]
[82189] (5)
protease C
1k7i
complexed with ca, zn; mutant
region a:259-479
[77281]
1k7q
complexed with ca, zn; mutant
region a:259-479
[77283]
1go8
complexed with ca, po4, zn; mutant
region p:259-479
[76247]
1k7g
complexed with ca, po4, zn
region a:259-479
[77279]
1go7
complexed with ca, po4, zn; mutant
region p:259-479
[76245]
Pseudomonas sp., tac ii 18
[TaxId: 306]
[82190] (8)
psychrophilic alkaline protease
1g9k
complexed with ca, so4, zn
region a:245-463
[76217]
1om8
complexed with ca, so4
region a:245-463
[87075]
1om6
complexed with ca, so4
region a:245-463
[87071]
1h71
complexed with ca, zn
region p:245-463
[76704]
1o0q
complexed with ca, so4
region a:245-463
[86536]
1o0t
complexed with ca, so4
region a:245-463
[86544]
1omj
complexed with ca, so4, zn
region a:245-463
[87083]
1om7
complexed with ca, so4
region a:245-463
[87073]
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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