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3PFY

The catalytic domain of human OTUD5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PEG A 400
ChainResidue
AASP238
AHOH460
AGLU241
AGLU241
AVAL242
AVAL242
AHOH404
AHOH404
AHOH417
AHOH460

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 401
ChainResidue
ALYS216
AASP231
AGLN232
AGLY235
AVAL334
AHOH439
AHOH447

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PG4 A 402
ChainResidue
AGLU197
AGLN199
ATRP202
ATYR257

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
ALYS219
AARG227
AHOH449
AHOH484

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AASP221

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:22245969, ECO:0000269|PubMed:33110214
ChainResidueDetails
ACYS224

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:22245969
ChainResidueDetails
AVAL334

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:22245969
ChainResidueDetails
ATYR175

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:22245969, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER177

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:33110214
ChainResidueDetails
ATHR195

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by MTOR => ECO:0000269|PubMed:33110214
ChainResidueDetails
AILE328

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:33110214
ChainResidueDetails
AASN337

222415

PDB entries from 2024-07-10

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