Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2Y5B

Structure of USP21 in complex with linear diubiquitin-aldehyde

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
E0004843molecular_functioncysteine-type deubiquitinase activity
E0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1000
ChainResidue
ACYS384
ACYS387
ACYS437
ACYS440

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 1559
ChainResidue
ASER472
AILE473

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1560
ChainResidue
AVAL514
FARG54
ALYS474
ALYS475
ASER513

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 E 1560
ChainResidue
EPRO235
ELYS369
EARG457

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 E 1561
ChainResidue
EGLU276
EALA277

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 1561
ChainResidue
AARG320

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1562
ChainResidue
APRO235
ALYS369
AARG457

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1563
ChainResidue
APRO483
ALEU484
AGLN485

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 E 1562
ChainResidue
EARG320

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1564
ChainResidue
ASER541
AASN543
EGLY296

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 1152
ChainResidue
AHIS515
BGLN116
BARG150

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 F 1152
ChainResidue
FGLN116
FARG148
FARG150

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1565
ChainResidue
AARG215
AASN216
AARG390
AASP534
ASER535

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 1000
ChainResidue
ECYS384
ECYS387
ECYS437
ECYS440

Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
BLYS27-ASP52
BLYS103-ASP128

site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLrnlGNtCFLNAvLQ
ChainResidueDetails
AGLY213-GLN228

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YqLyALcnHsGsvhy..GHY
ChainResidueDetails
ATYR502-TYR519

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10799498","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"32011234","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
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 Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21399617","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2Y5B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues75
DetailsDomain: {"description":"Ubiquitin-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon