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1A41

TYPE 1-TOPOISOMERASE CATALYTIC FRAGMENT FROM VACCINIA VIRUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003917molecular_functionDNA topoisomerase type I (single strand cut, ATP-independent) activity
A0006265biological_processDNA topological change
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AARG84
ALYS257
ASER268
ASER270
ALYS271

Functional Information from PROSITE/UniProt
site_idPS00176
Number of Residues19
DetailsTOPO_IB_1 Topoisomerase (Topo) IB-type active site signature. EvvghtpSISKraYMattI
ChainResidueDetails
AGLU261-ILE279

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"O-(3'-phospho-DNA)-tyrosine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01382","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10130","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15755148","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Involved in religation","evidences":[{"source":"UniProtKB","id":"P32989","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 9224599, 16487540, 9079646, 10820030, 16885024, 18367446, 2557629, 9529259
ChainResidueDetails
ATYR274
AARG223
AHIS265
ALYS167

site_idMCSA1
Number of Residues4
DetailsM-CSA 232
ChainResidueDetails
ALYS167attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay
AARG223attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
AHIS265electrostatic stabiliser, hydrogen bond donor
ATYR274hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

243083

PDB entries from 2025-10-15

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