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1RG1

Crystal structure of human Tyrosyl-DNA Phosphodiesterase complexed with vanadate, octopamine, and tetranucleotide AGTT

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0006281biological_processDNA repair
A0008081molecular_functionphosphoric diester hydrolase activity
B0005634cellular_componentnucleus
B0006281biological_processDNA repair
B0008081molecular_functionphosphoric diester hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE VO4 A 699
ChainResidue
AHIS263
ALYS265
AASN283
AHIS493
ALYS495
AASN516
AOTS997
DDT806

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE VO4 B 699
ChainResidue
BLYS265
BASN283
BHIS493
BLYS495
BASN516
BHOH676
BOTS998
FDT806
BHIS263

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SPM A 999
ChainResidue
AMET604
ATRP605
AVAL606
APRO607
BTHR449
BLEU451
BTHR600
BHIS601

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OTS A 997
ChainResidue
ATYR204
AGLY458
ASER459
APRO461
AHIS493
AVO4699
AHOH706
DDT806

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OTS B 998
ChainResidue
BTYR204
BASN283
BGLY458
BSER459
BHIS493
BHOH676
BVO4699
FDT806

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:12470949, ECO:0000269|PubMed:15111055
ChainResidueDetails
AHIS263
BHIS263

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:12470949, ECO:0000269|PubMed:15111055
ChainResidueDetails
AHIS493
BHIS493

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12470949
ChainResidueDetails
ALYS265
ALYS495
BLYS265
BLYS495

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Interaction with DNA => ECO:0000269|PubMed:12470949
ChainResidueDetails
ASER518
BSER518

223790

PDB entries from 2024-08-14

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