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4ZZX

Structure of PARP2 catalytic domain bound to an isoindolinone inhibitor

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 Residues10
DetailsBINDING SITE FOR RESIDUE FSU A 1584
ChainResidue
ASER328
AHOH2163
AHIS428
AGLY429
AGLY454
ATYR462
APHE463
ASER470
ATYR473
AHOH2162

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE FSU B 1584
ChainResidue
BSER328
BILE331
BHIS428
BGLY429
BGLY454
BTYR462
BPHE463
BSER470
BTYR473
BHOH2149

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
AARG444
ASER470
BHIS428
BGLY437
BARG444
BSER470
AHIS428
AGLY437

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
BSER226
BSER232
ASER226
ASER232

218500

PDB entries from 2024-04-17

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