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6JLQ

Crystal structure of human USP46-WDR48-WDR20 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0016579biological_processprotein deubiquitination
A0031647biological_processregulation of protein stability
A0032228biological_processregulation of synaptic transmission, GABAergic
A0045202cellular_componentsynapse
A0090263biological_processpositive regulation of canonical Wnt signaling pathway
A0098978cellular_componentglutamatergic synapse
A0099149biological_processregulation of postsynaptic neurotransmitter receptor internalization
A0101005molecular_functiondeubiquitinase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ZN A 401
ChainResidue
ACYS182
ACYS185
ACYS229
ATHR231
ACYS232

site_idAC2
Number of Residues1
Detailsbinding site for residue GOL A 402
ChainResidue
ALYS256

site_idAC3
Number of Residues3
Detailsbinding site for residue PO4 B 601
ChainResidue
BARG193
BLYS202
BLYS205

site_idAC4
Number of Residues2
Detailsbinding site for residue GOL B 602
ChainResidue
BSER238
BGLN241

site_idAC5
Number of Residues1
Detailsbinding site for residue GOL B 603
ChainResidue
BMET110

site_idAC6
Number of Residues1
Detailsbinding site for residue GOL B 604
ChainResidue
BHIS105

site_idAC7
Number of Residues5
Detailsbinding site for residue GOL B 605
ChainResidue
BASN261
BHIS266
BTYR268
BPRO309
BHIS330

site_idAC8
Number of Residues5
Detailsbinding site for residue GOL B 606
ChainResidue
BARG139
BLEU164
BSER165
BGLY166
BASN167

site_idAC9
Number of Residues1
Detailsbinding site for residue GOL B 607
ChainResidue
BARG274

site_idAD1
Number of Residues3
Detailsbinding site for residue GOL C 601
ChainResidue
CASP63
CLEU542
CASP544

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LISAssDtTVKVWNA
ChainResidueDetails
BLEU90-ALA104
BVAL132-VAL146

site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLvnfGNtCYCNSvLQ
ChainResidueDetails
AGLY36-GLN51

site_idPS00973
Number of Residues19
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YdLvAVvvHcGsgpnr.GHY
ChainResidueDetails
ATYR296-TYR314

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10093","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26388029","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22043315","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10093","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PDB","id":"5CVM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5CVN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5CVO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L8H","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues39
DetailsRepeat: {"description":"WD 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues39
DetailsRepeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues39
DetailsRepeat: {"description":"WD 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues39
DetailsRepeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues39
DetailsRepeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues39
DetailsRepeat: {"description":"WD 6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues39
DetailsRepeat: {"description":"WD 8","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BH57","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues44
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues71
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues41
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues35
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails

251801

PDB entries from 2026-04-08

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