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3IHP

Covalent Ubiquitin-Usp5 Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0004843molecular_functioncysteine-type deubiquitinase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005764cellular_componentlysosome
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
A0008270molecular_functionzinc ion binding
A0016567biological_processprotein ubiquitination
A0016579biological_processprotein deubiquitination
A0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
A0043130molecular_functionubiquitin binding
A0046872molecular_functionmetal ion binding
A0071108biological_processprotein K48-linked deubiquitination
A0101005molecular_functiondeubiquitinase activity
A2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
B0004197molecular_functioncysteine-type endopeptidase activity
B0004843molecular_functioncysteine-type deubiquitinase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005764cellular_componentlysosome
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
B0008270molecular_functionzinc ion binding
B0016567biological_processprotein ubiquitination
B0016579biological_processprotein deubiquitination
B0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
B0043130molecular_functionubiquitin binding
B0046872molecular_functionmetal ion binding
B0071108biological_processprotein K48-linked deubiquitination
B0101005molecular_functiondeubiquitinase activity
B2000059biological_processnegative regulation of ubiquitin-dependent protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NEH C 76
ChainResidue
AASN333
ACYS335
AGLN433
AGLY794
CGLY75

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NEH D 76
ChainResidue
DGLY75
BASN333
BCYS335
BGLN433
BGLY794

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL D 77
ChainResidue
DARG74

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 836
ChainResidue
ACYS199
ACYS202
ACYS219
AHIS232

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 836
ChainResidue
BCYS199
BCYS202
BCYS219
BHIS232

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS27-ASP52

site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GIrnlGNsCYLNSvVQ
ChainResidueDetails
AGLY327-GLN342

site_idPS00973
Number of Residues19
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YqLfAFisHmGtstmc.GHY
ChainResidueDetails
ATYR778-TYR796

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues216
DetailsZN_FING: UBP-type; degenerate => ECO:0000255|PROSITE-ProRule:PRU00502
ChainResidueDetails
AGLN175-MET283
BGLN175-MET283
DARG54
DARG72

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ACYS335
BCYS335

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093
ChainResidueDetails
AGLU818
BGLU818

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00502
ChainResidueDetails
ACYS199
ACYS202
ACYS219
AHIS232
BCYS199
BCYS202
BCYS219
BHIS232

site_idSWS_FT_FI5
Number of Residues10
DetailsBINDING:
ChainResidueDetails
ATRP209
BASP264
AARG221
ATYR259
ATYR261
AASP264
BTRP209
BARG221
BTYR259
BTYR261

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2
BALA2
DLYS63

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER156
BSER156
DLYS11
DLYS48

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR292
BTHR292

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P56399
ChainResidueDetails
ATHR623
BTHR623

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
AGLN779
ASER785
BGLN779
BSER785

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
APHE783
BPHE783

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PDB entries from 2024-07-24

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