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4B0S

Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005524molecular_functionATP binding
A0008233molecular_functionpeptidase activity
A0010498biological_processproteasomal protein catabolic process
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0019941biological_processmodification-dependent protein catabolic process
A0046872molecular_functionmetal ion binding
A0070490biological_processprotein pupylation
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue ATP A 1501
ChainResidue
AVAL4
ATHR102
APRO103
AASN157
ALEU159
AARG227
APRO230
AARG239
AARG433
ATRP453
AMG1502
AGLY6
AMG1503
AHOH2001
AILE7
AGLU8
AARG90
ATYR92
AASP94
AGLU99
ASER101

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 1502
ChainResidue
AGLU8
AHIS155
AHIS241
AATP1501
AMG1503

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 1503
ChainResidue
AGLU8
ATYR92
AGLU99
AATP1501
AMG1502
AHOH2001

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:22910360
ChainResidueDetails
AASP94

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:22910360
ChainResidueDetails
AGLU8
ATYR92
AGLU99
ASER101
AHIS155
AASN157
AARG239
AHIS241

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PDB entries from 2024-04-24

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