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1ECL

AMINO TERMINAL 67KDA DOMAIN OF ESCHERICHIA COLI DNA TOPOISOMERASE I (RESIDUES 2-590 OF MATURE PROTEIN) CLONING ARTIFACT ADDS TWO RESIDUES TO THE AMINO-TERMINUS WHICH WERE NOT OBSERVED IN THE EXPERIMENTAL ELECTRON DENSITY (GLY-2, SER-1).

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003916molecular_functionDNA topoisomerase activity
A0003917molecular_functionDNA topoisomerase type I (single strand cut, ATP-independent) activity
A0006265biological_processDNA topological change
Functional Information from PDB Data
site_idTY3
Number of Residues1
DetailsACTIVE SITE TYROSINE INVOLVED IN MAKING PHOSPHOTYROSINE COVALENT LINKAGE WITH DNA DURING CATALYSIS
ChainResidue
ATYR319

Functional Information from PROSITE/UniProt
site_idPS00396
Number of Residues15
DetailsTOPO_IA_1 Topoisomerase (Topo) IA-type active site signature. QrLYEagy.........ITYmRTD
ChainResidueDetails
AGLN309-ASP323

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: O-(5'-phospho-DNA)-tyrosine intermediate => ECO:0000255|PROSITE-ProRule:PRU01383, ECO:0000269|PubMed:21482796, ECO:0000269|PubMed:8114910, ECO:0000269|PubMed:9497321
ChainResidueDetails
ATYR319

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00952
ChainResidueDetails
AGLU9

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AASP111

site_idSWS_FT_FI4
Number of Residues8
DetailsSITE: Interaction with DNA
ChainResidueDetails
AHIS33
AARG168
AARG169
AASP172
ATYR177
ATRP184
AARG321
AARG507

Catalytic Information from CSA
site_idCSA1
Number of Residues3
Detailsa catalytic site defined by CSA, PubMed 9497321, 8114910, 20210704, 11809772
ChainResidueDetails
ATYR319
AGLU9
AARG321

site_idMCSA1
Number of Residues7
DetailsM-CSA 366
ChainResidueDetails
AGLU9electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, metal ligand, proton acceptor, proton donor, proton relay
AASP111electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, metal ligand, proton acceptor, proton donor, proton relay
AASP113metal ligand
AGLU115metal ligand
ATYR319activator, covalently attached, hydrogen bond acceptor, nucleofuge, nucleophile, proton acceptor, proton donor
AARG321electrostatic stabiliser
AHIS365electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity, proton acceptor, proton donor

227111

PDB entries from 2024-11-06

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