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1CY2

COMPLEX OF E.COLI DNA TOPOISOMERASE I WITH TPTPTP3'

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_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 700
ChainResidue
AARG202
AALA458
AARG535
AASN539
AHOH741

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TMP A 600
ChainResidue
AGLN165
AARG168
AARG321
ASER495
AHOH844
AASP113
AARG114
AGLU115
AARG161

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TMP A 601
ChainResidue
ASER294
ATHR295
ASER478
AALA480
ASER481
AARG515
AARG516
AHOH755

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 Residues4
DetailsAnnotated By Reference To The Literature 1ecl
ChainResidueDetails
AASP111
ATYR319
AGLU9
AHIS365

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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