Structural Classification of Proteins
Protein: Retroviral integrase, catalytic domain from Human immunodeficiency virus type 1
[TaxId: 11676]
Lineage:
Root:
scop
Class:
Alpha and beta proteins (a/b)
[51349]
Mainly parallel beta sheets (beta-alpha-beta units)
Fold:
Ribonuclease H-like motif
[53066]
3 layers: a/b/a; mixed beta-sheet of 5 strands, order 32145; strand 2 is antiparallel to the rest
Superfamily:
Ribonuclease H-like
[53098]
consists of one domain of this fold
uperfamily
Family:
Retroviral integrase, catalytic domain
[53107]
Protein: Retroviral integrase, catalytic domain [53108]
Species:
Human immunodeficiency virus type 1
[TaxId: 11676]
[53110]
PDB Entry Domains:
1exq
complexed with cd, cl, so4; mutant
chain a
[33646]
chain b
[33647]
1hyv
complexed with caf, cl, so4, tta; mutant
chain a
[61424]
1b9d
complexed with cac, so4; mutant
chain a
[33649]
1b9f
complexed with cac, so4; mutant
chain a
[33648]
2b4j
automatically matched to d1biza_
complexed with gol, po4; mutant
region a:57-208
[127833]
2b4j
automatically matched to d1biza_
complexed with gol, po4; mutant
region b:57-208
[127834]
1b92
complexed with cac, so4; mutant
chain a
[33654]
1bis
mutant
chain a
[33650]
chain b
[33651]
1biz
complexed with cac; mutant
chain a
[33652]
chain b
[33653]
1bl3
complexed with mg; mutant
chain a
[33655]
chain b
[33656]
chain c
[33657]
1qs4
chain a
[33658]
chain b
[33659]
chain c
[33660]
1itg
complexed with cac; mutant
chain a
[33661]
1biu
complexed with mg; mutant
chain a
[33663]
chain b
[33664]
chain c
[33665]
1hyz
complexed with caf, cl, so4, tto; mutant
chain a
[61426]
1k6y
complexed with k, po4, zn; mutant
region a:56-210
[68240]
region b:56-212
[68242]
region c:56-209
[68244]
region d:56-211
[68246]
1bhl
complexed with cas; mutant
chain a
[33662]
1bi4
mutant
chain a
[33666]
chain b
[33667]
chain c
[33668]
1ex4
complexed with cps; mutant
region a:56-222
[33670]
region b:55-222
[33671]
2itg
mutant
chain a
[33669]
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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