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4PJV

Structure of PARP2 catalytic domain bound to inhibitor BMN 673

Functional Information from GO Data
ChainGOidnamespacecontents
A0003950molecular_functionNAD+ ADP-ribosyltransferase activity
B0003950molecular_functionNAD+ ADP-ribosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue 2YQ A 601
ChainResidue
ASER328
ALYS469
ASER470
ATYR473
AGLU558
AGOL602
AHOH729
AHOH756
AHOH765
AGLN332
AGLU335
AHIS428
AGLY429
AGLY454
ATYR455
ATYR462
APHE463

site_idAC2
Number of Residues8
Detailsbinding site for residue GOL A 602
ChainResidue
AGLU335
AASP339
AHIS428
ASER430
ALEU443
AARG444
A2YQ601
AHOH765

site_idAC3
Number of Residues6
Detailsbinding site for residue GOL A 603
ChainResidue
AASP396
ATYR397
AALA471
AASN472
APHE475
AALA476

site_idAC4
Number of Residues16
Detailsbinding site for residue 2YQ B 601
ChainResidue
BSER328
BGLN332
BGLU335
BHIS428
BGLY429
BGLY454
BTYR462
BPHE463
BALA464
BLYS469
BSER470
BTYR473
BGLU558
BHOH723
BHOH726
BHOH741

site_idAC5
Number of Residues5
Detailsbinding site for residue GOL B 602
ChainResidue
BASP396
BALA471
BASN472
BPHE475
BALA476

Functional Information from PROSITE/UniProt
site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. LLEANPKA
ChainResidueDetails
ALEU498-ALA505

site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HgsrmSnwVgILSHG
ChainResidueDetails
AHIS428-GLY442

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:26704974, ECO:0000305|PubMed:30104678, ECO:0000305|PubMed:32028527
ChainResidueDetails
AGLU558
BGLU558

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:32028527, ECO:0007744|PDB:6TX3
ChainResidueDetails
AHIS428
AGLY437
AARG444
ASER470
BHIS428
BGLY437
BARG444
BSER470

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PDB entries from 2024-08-28

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