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6VKK

Crystal Structure of human PARP-1 CAT domain bound to inhibitor rucaparib

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 PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue RPB A 1101
ChainResidue
AGLU763
ALYS903
ASER904
ATYR907
AGLU988
AHOH1209
AHOH1230
AASP766
AHIS862
AGLY863
AGLY888
ATYR889
ATYR896
APHE897
AALA898

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 1102
ChainResidue
AGLY843
AGLU844
ACYS845
AGLN846
CGLU842
CGLY843
CGLN846

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 1103
ChainResidue
ALYS943
BLYS838
BLYS1000
DGLN846
DLYS849

site_idAC4
Number of Residues5
Detailsbinding site for residue SO4 A 1104
ChainResidue
ALYS903
ALEU984
ALEU985
ATYR986
AHOH1201

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 1105
ChainResidue
AARG858
AMET929
ALYS949

site_idAC6
Number of Residues13
Detailsbinding site for residue RPB D 1101
ChainResidue
DGLU763
DASP766
DHIS862
DGLY863
DGLY888
DTYR889
DTYR896
DPHE897
DALA898
DLYS903
DSER904
DTYR907
DGLU988

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL D 1102
ChainResidue
BGLY843
BCYS845
BGLN846
DGLY843
DGLU844
DCYS845
DGLN846

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 D 1103
ChainResidue
DLYS903
DLEU984
DLEU985
DTYR986

site_idAC9
Number of Residues14
Detailsbinding site for residue RPB C 1101
ChainResidue
CGLN759
CGLU763
CHIS862
CGLY863
CGLY888
CTYR889
CTYR896
CPHE897
CALA898
CLYS903
CSER904
CTYR907
CGLU988
CHOH1210

site_idAD1
Number of Residues5
Detailsbinding site for residue SO4 C 1102
ChainResidue
AGLN846
ALYS849
CLYS838
CLYS1000
DLYS943

site_idAD2
Number of Residues4
Detailsbinding site for residue SO4 C 1103
ChainResidue
CLYS903
CLEU984
CLEU985
CTYR986

site_idAD3
Number of Residues3
Detailsbinding site for residue SO4 C 1104
ChainResidue
CARG858
CMET929
CLYS949

site_idAD4
Number of Residues4
Detailsbinding site for residue GOL B 1201
ChainResidue
BGLY944
BHIS946
CGLY944
CHIS946

site_idAD5
Number of Residues14
Detailsbinding site for residue RPB B 1202
ChainResidue
BSER904
BTYR907
BGLU988
BHOH1313
BGLN759
BGLU763
BHIS862
BGLY863
BTHR887
BTYR889
BTYR896
BPHE897
BALA898
BLYS903

site_idAD6
Number of Residues4
Detailsbinding site for residue SO4 B 1203
ChainResidue
BLYS903
BLEU984
BLEU985
BTYR986

site_idAD7
Number of Residues5
Detailsbinding site for residue SO4 B 1204
ChainResidue
BARG858
BMET929
BLYS949
BHOH1307
DGLY978

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
DGLU988
CGLU988
BGLU988

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

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
ASER782
DSER782
CSER782
BSER782

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER786
DSER786
CSER786
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
ALYS748
DLYS748
CLYS748
BLYS748

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PDB entries from 2024-06-19

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