Structural Classification of Proteins
Protein: multi-copper oxidase CueO from Escherichia coli
[TaxId: 562]
Lineage:
Root:
scop
Class:
All beta proteins
[48724]
Fold:
Cupredoxin-like
[49502]
sandwich; 7 strands in 2 sheets, greek-key
variations: some members have additional 1-2 strands
Superfamily:
Cupredoxins
[49503]
contains copper-binding site
uperfamily
Family:
Multidomain cupredoxins
[49550]
Protein: multi-copper oxidase CueO [69194]
Species:
Escherichia coli
[TaxId: 562]
[69195]
PDB Entry Domains:
1kv7
complexed with c2o, cu
region a:31-170
[68873]
region a:171-335
[68874]
region a:336-516
[68875]
1pf3
complexed with c2c, cu; mutant
region a:31-170
[88049]
region a:171-335
[88050]
region a:336-516
[88051]
1n68
complexed with c2c, cu
region a:30-170
[85356]
region a:171-335
[85357]
region a:336-516
[85358]
2fqe
automatically matched to d1n68a1
complexed with c2o, cit, cu, na
region a:31-170
[133946]
2fqe
automatically matched to d1kv7a2
complexed with c2o, cit, cu, na
region a:171-335
[133947]
2fqe
automatically matched to d1kv7a3
complexed with c2o, cit, cu, na
region a:336-516
[133948]
2fqf
automatically matched to d1n68a1
complexed with c2o, cit, cu
region a:31-170
[133949]
2fqf
automatically matched to d1kv7a2
complexed with c2o, cit, cu
region a:171-335
[133950]
2fqf
automatically matched to d1kv7a3
complexed with c2o, cit, cu
region a:336-516
[133951]
2fqd
automatically matched to d1n68a1
complexed with c2o, cit, cu
region a:30-170
[133943]
2fqd
automatically matched to d1kv7a2
complexed with c2o, cit, cu
region a:171-335
[133944]
2fqd
automatically matched to d1kv7a3
complexed with c2o, cit, cu
region a:336-516
[133945]
2fqg
automatically matched to d1n68a1
complexed with c2o, cit, cu, na, pge
region a:31-170
[133952]
2fqg
automatically matched to d1kv7a2
complexed with c2o, cit, cu, na, pge
region a:171-335
[133953]
2fqg
automatically matched to d1kv7a3
complexed with c2o, cit, cu, na, pge
region a:336-516
[133954]
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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