Structural Classification of Proteins
Fold: FYVE/PHD zinc finger
dimetal(zinc)-bound alpha+beta fold
Lineage:
Root:
scop
Class:
Small proteins
[56992]
Usually dominated by metal ligand, heme, and/or disulfide bridges
Fold:
FYVE/PHD zinc finger
[57902]
dimetal(zinc)-bound alpha+beta fold
Superfamilies:
FYVE/PHD zinc finger
[57903] (3)
uperfamily
FYVE, a phosphatidylinositol-3-phosphate binding domain
[57904] (6)
vps27p protein [57905]
Baker's yeast (Saccharomyces cerevisiae)
[TaxId: 4932]
[57906] (1)
1vfy
complexed with zn; mutant
chain a
[45357]
Eea1 [64583]
Human (Homo sapiens)
[TaxId: 9606]
[64584] (3)
1joc
complexed with itp, zn
region a:1348-1411
[66990]
region b:1348-1411
[66992]
1hyi
complexed with inositol 1,3-bisphosphate
complexed with itp, zn
chain a
[61406]
1hyj
complexed with zn
chain a
[61407]
Hrs [57907]
protein involved in membrane trafficking and signal transduction
Fruit fly (Drosophila melanogaster)
[TaxId: 7227]
[57908] (1)
1dvp
complexed with cit, zn
region a:149-220
[45358]
Effector domain of rabphilin-3a [57909]
contains additional N-terminal long alpha-helix
Rat (Rattus norvegicus)
[TaxId: 10116]
[57910] (1)
1zbd
complexed with gtp, mg, zn; mutant
chain b
[45359]
Zinc finger FYVE domain containing protein 19 [118324]
Mouse (Mus musculus)
[TaxId: 10090]
[118325] (1)
SQ
Q9DAZ9
1-75
1wfk
Structural genomics target
complexed with zn
chain a
[114585]
Rififylin (FYVE-RING finger protein Sakura) [118326]
Human (Homo sapiens)
[TaxId: 9606]
[118327] (1)
SQ
Q8WZ73
45-139
1y02
complexed with zn
region a:20-70
[116279]
PHD domain
[57911] (14)
Williams-Beuren syndrome transcription factor, WSTF [57912]
Human (Homo sapiens)
[TaxId: 9606]
[57913] (1)
1f62
complexed with zn
chain a
[45360]
Nuclear corepressor KAP-1 (TIF-1beta) [57914]
Human (Homo sapiens)
[TaxId: 9606]
[57915] (1)
1fp0
complexed with zn
region a:19-88
[45361]
Mi2-beta (CHD4) [90226]
chromodomain-helicase-DNA-binding protein 4
Human (Homo sapiens)
[TaxId: 9606]
[90227] (2)
1mm3
second PHD domain with the C-terminal loop replaced by the corresponding loop from WSTF
complexed with zn
chain a
[85016]
1mm2
second PHD domain
complexed with zn
chain a
[85015]
PHD finger protein At5g26210 [118328]
Thale cress (Arabidopsis thaliana)
[TaxId: 3702]
[118329] (1)
SQ
O81488
201-251
1we9
Structural genomics target
complexed with zn
chain a
[114549]
PHD finger protein At1g33420 [118330]
Thale cress (Arabidopsis thaliana)
[TaxId: 3702]
[118331] (1)
SQ
Q9C810
595-653
1wee
Structural genomics target
complexed with zn
chain a
[114550]
Death associated transcription factor 1, Datf1 (DIO-1) [118332]
Mouse (Mus musculus)
[TaxId: 10090]
[118333] (1)
SQ
Q8C9B9
257-319
1wem
Structural genomics target
complexed with zn
chain a
[114559]
Inhibitor of growth protein 4, Ing4 [118334]
Mouse (Mus musculus)
[TaxId: 10090]
[118335] (2)
SQ
Q8C0D7
188-245
1wen
Structural genomics target
complexed with zn
chain a
[114560]
1weu
Structural genomics target; the extra N-terminal region (168-187) is unstructured
complexed with zn
chain a
[114565]
Homo sapiens
[TaxId: 9606]
[161223] (5)
2pnx
automatically matched to d1wena_
complexed with m3l, zn
region a:195-245
[149708]
2vnf
automatically matched to d1wena_
complexed with dtt, dtu, m3l, na, zn
region a:195-244
[153333]
2vnf
automatically matched to d1wena_
complexed with dtt, dtu, m3l, na, zn
region c:191-244
[153334]
2pnx
automatically matched to d1wena_
complexed with m3l, zn
region c:195-244
[149709]
2k1j
automatically matched to d1wena_
complexed with zn
region a:188-245
[148257]
PHD finger protein 8 [118336]
Mouse (Mus musculus)
[TaxId: 10090]
[118337] (1)
SQ
Q80TJ7
1-66
1wep
Structural genomics target
complexed with zn
chain a
[114562]
PHD finger protein 7 (NYD-SP6) [118338]
Mouse (Mus musculus)
[TaxId: 10090]
[118339] (1)
SQ
Q9DAG9
232-304
1weq
Structural genomics target
complexed with zn
chain a
[114563]
PHD Inhibitor of growth protein 2, Ing2 [118340]
Mouse (Mus musculus)
[TaxId: 10090]
[118341] (1)
SQ
Q9ESK4
205-262
1wes
Structural genomics target
complexed with zn
chain a
[114564]
PHD finger protein 22 [118342]
Mouse (Mus musculus)
[TaxId: 10090]
[118343] (1)
SQ
Q9D168
150-224
1wev
Structural genomics target
complexed with zn
chain a
[114566]
Sumoylation ligase E3, SIZ1 [118344]
Thale cress (Arabidopsis thaliana)
[TaxId: 3702]
[118345] (1)
SQ
Q680Q4
104-168
1wew
Structural genomics target
complexed with zn
chain a
[114567]
V(D)J recombination-activating protein 2, Rag2 [161224]
Mouse (Mus musculus)
[TaxId: 10090]
[161225] (14)
SQ
P21784
414-487
2v89
automatically matched to 2JWO A:414-487
complexed with m3l, zn
region a:1414-1487
[152778]
2v89
automatically matched to 2JWO A:414-487
complexed with m3l, zn
region b:414-487
[152779]
2v86
automatically matched to 2JWO A:414-487
complexed with da2, m3l, zn
region a:414-487
[152772]
2v86
automatically matched to 2JWO A:414-487
complexed with da2, m3l, zn
region b:414-487
[152773]
2v87
automatically matched to 2JWO A:414-487
complexed with 2mr, m3l, zn
region a:414-487
[152774]
2v87
automatically matched to 2JWO A:414-487
complexed with 2mr, m3l, zn
region b:414-487
[152775]
2v85
automatically matched to 2JWO A:414-487
complexed with m3l, nmm, zn
region a:414-487
[152770]
2v85
automatically matched to 2JWO A:414-487
complexed with m3l, nmm, zn
region b:414-487
[152771]
2v88
automatically matched to 2JWO A:414-487
complexed with 2mr, mly, zn
region a:414-487
[152776]
2v88
automatically matched to 2JWO A:414-487
complexed with 2mr, mly, zn
region b:414-487
[152777]
2v83
automatically matched to 2JWO A:414-487
complexed with m3l, zn
region a:414-485
[152767]
2v83
automatically matched to 2JWO A:414-487
complexed with m3l, zn
region b:414-487
[152768]
2v83
automatically matched to 2JWO A:414-487
complexed with m3l, zn
region c:414-483
[152769]
2jwo
complexed with zn
region a:414-487
[148229]
variant PHD-like domain
[118346] (1)
Hypothetical protein KIAA1045 [118347]
Human (Homo sapiens)
[TaxId: 9606]
[118348] (1)
SQ
Q9UPV7
123-198
1wil
Structural genomics target
complexed with zn
chain a
[114676]
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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