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7S6H

Human PARP1 deltaV687-E688 bound to NAD+ analog EB-47 and to a DNA double strand break.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0008270molecular_functionzinc ion binding
B0003950molecular_functionNAD+ ADP-ribosyltransferase activity
C0003677molecular_functionDNA binding
C0008270molecular_functionzinc ion binding
D0003950molecular_functionNAD+ ADP-ribosyltransferase activity
Functional Information from PROSITE/UniProt
site_idPS00347
Number of Residues36
DetailsZF_PARP_1 Zinc finger poly(ADP-ribose) polymerase (PARP)-type signature. CKkCsesIpKdslRmaimvqspmfdgkvph..WYHfsC
ChainResidueDetails
ACYS21-CYS56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues168
DetailsZN_FING: PARP-type 1 => ECO:0000255|PROSITE-ProRule:PRU00264
ChainResidueDetails
ATYR9-GLY203
CTYR9-GLY203

site_idSWS_FT_FI2
Number of Residues180
DetailsZN_FING: PARP-type 2 => ECO:0000255|PROSITE-ProRule:PRU00264
ChainResidueDetails
ALYS223-GLY313
CLYS223-GLY313
BALA880
BASN906
DSER864
DLEU873
DALA880
DASN906

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22582261, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3OD8, ECO:0007744|PDB:3ODA, ECO:0007744|PDB:4AV1, ECO:0007744|PDB:4DQY, ECO:0007744|PDB:4OPX, ECO:0007744|PDB:4OQA, ECO:0007744|PDB:4OQB
ChainResidueDetails
AHIS53
ACYS56
CCYS21
CCYS24
CHIS53
CCYS56
ACYS21
ACYS24

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00264, ECO:0000269|PubMed:21233213, ECO:0000269|PubMed:22683995, ECO:0007744|PDB:3ODC, ECO:0007744|PDB:3ODE, ECO:0007744|PDB:4AV1
ChainResidueDetails
ALYS269
AVAL272
CGLU235
CLEU238
CLYS269
CVAL272
AGLU235
ALEU238

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01351, ECO:0000269|PubMed:18055453, ECO:0000269|PubMed:22582261, ECO:0007744|PDB:2RIQ, ECO:0007744|PDB:4DQY, ECO:0007744|PDB:4OPX, ECO:0007744|PDB:4OQA, ECO:0007744|PDB:4OQB
ChainResidueDetails
CCYS311
CCYS321
ACYS311
ACYS321
CCYS295
CCYS298
ACYS295
ACYS298

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Cleavage; by caspase-3 and caspase-7 => ECO:0000269|PubMed:10497198, ECO:0000269|PubMed:22464733, ECO:0000269|PubMed:7596430
ChainResidueDetails
AASP214
CASP214

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.12, ECO:0007744|PubMed:22814378
ChainResidueDetails
DLYS600
DLYS621
AALA2
CALA2

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER41
CSER41

site_idSWS_FT_FI9
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AGLY215
AGLN241
CLYS207
CGLY215
CGLN241
ALYS207

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER277
CSER274
CSER277
ASER274
CMET287
CCYS295
AMET287
ACYS295

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17525332, ECO:0007744|PubMed:23186163
ChainResidueDetails
CPHE289
DPRO750
APHE289

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER364
CSER364

site_idSWS_FT_FI13
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS249
CLEU302
CLYS249
ALEU302

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733
ChainResidueDetails
CGLY313
AGLY313

221051

PDB entries from 2024-06-12

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