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3ODA

Human PARP-1 zinc finger 1 (Zn1) bound to DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0008270molecular_functionzinc ion binding
B0003677molecular_functionDNA binding
B0008270molecular_functionzinc ion binding
C0003677molecular_functionDNA binding
C0008270molecular_functionzinc ion binding
D0003677molecular_functionDNA binding
D0008270molecular_functionzinc ion binding
E0003677molecular_functionDNA binding
E0008270molecular_functionzinc ion binding
F0003677molecular_functionDNA binding
F0008270molecular_functionzinc ion binding
G0003677molecular_functionDNA binding
G0008270molecular_functionzinc ion binding
H0003677molecular_functionDNA binding
H0008270molecular_functionzinc ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 200
ChainResidue
ACYS21
ACYS24
AHIS53
ACYS56

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 200
ChainResidue
BCYS21
BCYS24
BHIS53
BCYS56

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 200
ChainResidue
CCYS24
CHIS53
CCYS56
CCYS21

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN D 200
ChainResidue
DCYS21
DCYS24
DHIS53
DCYS56

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN E 200
ChainResidue
ECYS21
ECYS24
EHIS53
ECYS56

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN F 200
ChainResidue
FCYS21
FCYS24
FHIS53
FCYS56

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G 200
ChainResidue
GCYS21
GCYS24
GHIS53
GCYS56

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN H 200
ChainResidue
HCYS21
HCYS24
HHIS53
HCYS56

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 Residues672
DetailsZN_FING: PARP-type 1 => ECO:0000255|PROSITE-ProRule:PRU00264
ChainResidueDetails
ATYR9-GLY93
BTYR9-GLY93
CTYR9-GLY93
DTYR9-GLY93
ETYR9-GLY93
FTYR9-GLY93
GTYR9-GLY93
HTYR9-GLY93

site_idSWS_FT_FI2
Number of Residues32
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
ACYS21
CCYS24
CHIS53
CCYS56
DCYS21
DCYS24
DHIS53
DCYS56
ECYS21
ECYS24
EHIS53
ACYS24
ECYS56
FCYS21
FCYS24
FHIS53
FCYS56
GCYS21
GCYS24
GHIS53
GCYS56
HCYS21
AHIS53
HCYS24
HHIS53
HCYS56
ACYS56
BCYS21
BCYS24
BHIS53
BCYS56
CCYS21

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.12, ECO:0007744|PubMed:22814378
ChainResidueDetails
AALA2
BALA2
CALA2
DALA2
EALA2
FALA2
GALA2
HALA2

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER41
BSER41
CSER41
DSER41
ESER41
FSER41
GSER41
HSER41

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PDB entries from 2024-07-10

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