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1RFF

Crystal structure of human Tyrosyl-DNA Phosphodiesterase complexed with vanadate, octapeptide KLNYYDPR, 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
CTYR723
DDT806

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE VO4 B 699
ChainResidue
BLYS265
BASN283
BHIS493
BLYS495
BASN516
ETYR723
FDT806
BHIS263

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SPM A 700
ChainResidue
AMET604
ATRP605
AVAL606
BTHR449
BSER450
BLEU451
BTHR600

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SPM B 700
ChainResidue
BMET604
BVAL606
BPRO607
BHOH1136

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

222415

PDB entries from 2024-07-10

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