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7KK5

Structure of the catalytic domain of PARP1 in complex with niraparib

Functional Information from GO Data
ChainGOidnamespacecontents
A0003950molecular_functionNAD+ ADP-ribosyltransferase activity
B0003950molecular_functionNAD+ ADP-ribosyltransferase activity
C0003950molecular_functionNAD+ ADP-ribosyltransferase activity
D0003950molecular_functionNAD+ ADP-ribosyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: For poly [ADP-ribose] polymerase activity => ECO:0000305|PubMed:32028527, ECO:0000305|PubMed:7852410, ECO:0000305|PubMed:9315851
ChainResidueDetails
AGLU988
BGLU988
CGLU988
DGLU988

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9UGN5
ChainResidueDetails
BHIS862
BGLY871
BARG878
BSER904
CHIS862
CGLY871
CARG878
CSER904
DHIS862
DGLY871
DARG878
DSER904
AGLY871
AARG878
ASER904
AHIS862

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER782
CSER782
DSER782
ASER782

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER786
DSER786
ASER786
BSER786

site_idSWS_FT_FI5
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS748
DLYS748
BLYS748
ALYS748

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PDB entries from 2024-06-12

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