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2BKQ

NEDD8 protease

Functional Information from GO Data
ChainGOidnamespacecontents
A0000338biological_processprotein deneddylation
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
A0016579biological_processprotein deubiquitination
A0019784molecular_functiondeNEDDylase activity
A0043687biological_processpost-translational protein modification
B0000338biological_processprotein deneddylation
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
B0016579biological_processprotein deubiquitination
B0019784molecular_functiondeNEDDylase activity
B0043687biological_processpost-translational protein modification
C0000338biological_processprotein deneddylation
C0005515molecular_functionprotein binding
C0005829cellular_componentcytosol
C0006508biological_processproteolysis
C0008234molecular_functioncysteine-type peptidase activity
C0016579biological_processprotein deubiquitination
C0019784molecular_functiondeNEDDylase activity
C0043687biological_processpost-translational protein modification
D0000338biological_processprotein deneddylation
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0006508biological_processproteolysis
D0008234molecular_functioncysteine-type peptidase activity
D0016579biological_processprotein deubiquitination
D0019784molecular_functiondeNEDDylase activity
D0043687biological_processpost-translational protein modification
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE:
ChainResidueDetails
AHIS102
AASP119
BHIS102
BASP119
CHIS102
CASP119
DHIS102
DASP119

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ACYS163
BCYS163
CCYS163
DCYS163

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895
ChainResidueDetails
AMET1
BMET1
CMET1
DMET1

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bkr
ChainResidueDetails
ATRP103
AHIS102
AASP119
ATRP26
ACYS163

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bkr
ChainResidueDetails
BTRP103
BHIS102
BASP119
BTRP26
BCYS163

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bkr
ChainResidueDetails
CTRP103
CHIS102
CASP119
CTRP26
CCYS163

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 2bkr
ChainResidueDetails
DTRP103
DHIS102
DASP119
DTRP26
DCYS163

site_idMCSA1
Number of Residues5
DetailsM-CSA 820
ChainResidueDetails
ATRP26electrostatic stabiliser
AHIS102proton acceptor, proton donor
ATRP103electrostatic stabiliser
AASP119electrostatic stabiliser
ACYS163nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues5
DetailsM-CSA 820
ChainResidueDetails
BTRP26electrostatic stabiliser
BHIS102proton acceptor, proton donor
BTRP103electrostatic stabiliser
BASP119electrostatic stabiliser
BCYS163nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA3
Number of Residues5
DetailsM-CSA 820
ChainResidueDetails
CTRP26electrostatic stabiliser
CHIS102proton acceptor, proton donor
CTRP103electrostatic stabiliser
CASP119electrostatic stabiliser
CCYS163nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA4
Number of Residues5
DetailsM-CSA 820
ChainResidueDetails
DTRP26electrostatic stabiliser
DHIS102proton acceptor, proton donor
DTRP103electrostatic stabiliser
DASP119electrostatic stabiliser
DCYS163nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-10-16

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