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5LRT

Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ADP and Phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
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 Residues26
Detailsbinding site for residue ADP A 601
ChainResidue
AGLY6
AGLU104
AASN157
ALEU159
AARG227
AGLU229
APRO230
AARG239
AHIS241
AARG433
ATRP453
AILE7
AMG602
AMG603
AMG604
APO4606
AHOH738
AHOH796
AHOH864
AGLU8
AARG90
ATYR92
AGLU99
ASER101
ATHR102
APRO103

site_idAC2
Number of Residues6
Detailsbinding site for residue MG A 602
ChainResidue
AGLU229
AADP601
AHOH721
AHOH738
AHOH796
AHOH864

site_idAC3
Number of Residues6
Detailsbinding site for residue MG A 603
ChainResidue
AGLU8
ATYR92
AGLU99
AADP601
AMG605
APO4606

site_idAC4
Number of Residues6
Detailsbinding site for residue MG A 604
ChainResidue
AGLU8
AHIS155
AARG227
AHIS241
AADP601
APO4606

site_idAC5
Number of Residues6
Detailsbinding site for residue MG A 605
ChainResidue
AGLU10
AASP94
AGLU99
AMG603
APO4606
AHOH840

site_idAC6
Number of Residues18
Detailsbinding site for residue PO4 A 606
ChainResidue
AGLU8
AGLU10
ATYR92
AASP94
AGLU99
AHIS155
AARG227
AHIS241
AADP601
AMG603
AMG604
AMG605
ANA611
AHOH726
AHOH748
AHOH779
AHOH840
AHOH856

site_idAC7
Number of Residues10
Detailsbinding site for residue P6G A 607
ChainResidue
ASER358
ASER368
AILE369
ALEU406
AARG409
AARG411
AGLY445
AALA446
AHOH776
AHOH822

site_idAC8
Number of Residues4
Detailsbinding site for residue PGE A 608
ChainResidue
ALEU113
ATHR423
APRO428
AASN430

site_idAC9
Number of Residues5
Detailsbinding site for residue PGE A 609
ChainResidue
AARG109
ATYR255
AMET335
ALEU415
AHOH704

site_idAD1
Number of Residues4
Detailsbinding site for residue PEG A 610
ChainResidue
APRO398
AGLU418
AHOH860
AHOH881

site_idAD2
Number of Residues7
Detailsbinding site for residue NA A 611
ChainResidue
AGLU10
ATHR217
ATHR218
APO4606
AHOH779
AHOH856
AHOH869

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 2024-09-11

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