Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5VSK

Structure of DUB complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
B0004843molecular_functioncysteine-type deubiquitinase activity
B0016579biological_processprotein deubiquitination
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue 9HS A 601
ChainResidue
ATYR224
AHIS456
ATYR465
ATYR514
AASP295
AVAL296
AGLN297
AGLN405
AMET407
AARG408
APHE409
ALYS420

site_idAC2
Number of Residues3
Detailsbinding site for residue ZN A 602
ChainResidue
ACYS300
AASP349
AHIS403

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 603
ChainResidue
AHIS464
AASP481
BASP459
BHIS461

site_idAC4
Number of Residues13
Detailsbinding site for residue 9HS B 601
ChainResidue
BTYR224
BASP295
BVAL296
BGLN297
BLEU406
BMET407
BARG408
BPHE409
BLYS420
BHIS456
BHIS461
BTYR465
BTYR514

site_idAC5
Number of Residues2
Detailsbinding site for residue ZN B 602
ChainResidue
BCYS300
BHIS403

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 603
ChainResidue
AASP459
AHIS461
BHIS464
BASP481

Functional Information from PROSITE/UniProt
site_idPS00972
Number of Residues16
DetailsUSP_1 Ubiquitin specific protease (USP) domain signature 1. GLknqGAtCYMNSlLQ
ChainResidueDetails
AGLY215-GLN230

site_idPS00973
Number of Residues18
DetailsUSP_2 Ubiquitin specific protease (USP) domain signature 2. YiLhAVlvHsGdnhg..GHY
ChainResidueDetails
ATYR448-TYR465

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:12507430, ECO:0000269|PubMed:25944111, ECO:0000305|PubMed:11923872, ECO:0000305|PubMed:15053880, ECO:0000305|PubMed:16964248, ECO:0000305|PubMed:18716620, ECO:0000305|PubMed:21745816, ECO:0000305|PubMed:22411829
ChainResidueDetails
AARG239
BARG239

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:12507430
ChainResidueDetails
APHE480
BPHE480

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
APHE234electrostatic stabiliser
AARG239nucleofuge, nucleophile, proton acceptor, proton donor
APHE480proton acceptor, proton donor
AASN497electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
BPHE234electrostatic stabiliser
BARG239nucleofuge, nucleophile, proton acceptor, proton donor
BPHE480proton acceptor, proton donor
BASN497electrostatic stabiliser

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon