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1NBF

Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde

Functional Information from GO Data
ChainGOidnamespacecontents
A0004843molecular_functioncysteine-type deubiquitinase activity
A0016579biological_processprotein deubiquitination
B0004843molecular_functioncysteine-type deubiquitinase activity
B0016579biological_processprotein deubiquitination
E0004843molecular_functioncysteine-type deubiquitinase activity
E0016579biological_processprotein deubiquitination
Functional Information from PROSITE/UniProt
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
CLYS327-ASP352

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 Residues4
DetailsSITE: Interacts with activating enzyme
ChainResidueDetails
CARG354
CARG372
DARG354
DARG372

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Essential for function
ChainResidueDetails
CHIS368
DHIS368
EHIS464

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291
ChainResidueDetails
CSER365
DSER365

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457
ChainResidueDetails
CTHR366
DTHR366

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742
ChainResidueDetails
CGLZ376
DGLZ376

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603
ChainResidueDetails
CLYS306
DLYS306

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
ChainResidueDetails
CGLZ376
DGLZ376

site_idSWS_FT_FI8
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144
ChainResidueDetails
CLYS311
CLYS348
DLYS311
DLYS348

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860
ChainResidueDetails
CLYS327
DLYS327

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127
ChainResidueDetails
CLYS329
DLYS329

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577
ChainResidueDetails
CLYS333
DLYS333

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106
ChainResidueDetails
CLYS363
DLYS363

Catalytic Information from CSA
site_idCSA1
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 12507430
ChainResidueDetails
AASN218
ACYS223
ACYS223
AASP481
AHIS464

site_idCSA2
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 12507430
ChainResidueDetails
BASN218
BCYS223
BCYS223
BASP481
BHIS464

site_idCSA3
Number of Residues5
Detailsa catalytic site defined by CSA, PubMed 12507430
ChainResidueDetails
EASN218
ECYS223
ECYS223
EASP481
EHIS464

site_idMCSA1
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
AASN218electrostatic stabiliser
ACYS223nucleofuge, nucleophile, proton acceptor, proton donor
AHIS464proton acceptor, proton donor
AASP481electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
BASN218electrostatic stabiliser
BCYS223nucleofuge, nucleophile, proton acceptor, proton donor
BHIS464proton acceptor, proton donor
BASP481electrostatic stabiliser

site_idMCSA3
Number of Residues4
DetailsM-CSA 789
ChainResidueDetails
EASN218electrostatic stabiliser
ECYS223nucleofuge, nucleophile, proton acceptor, proton donor
EHIS464proton acceptor, proton donor
EASP481electrostatic stabiliser

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PDB entries from 2024-07-24

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