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1AKO

EXONUCLEASE III FROM ESCHERICHIA COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004527molecular_functionexonuclease activity
A0005829cellular_componentcytosol
A0006281biological_processDNA repair
A0006974biological_processDNA damage response
A0008311molecular_functiondouble-stranded DNA 3'-5' DNA exonuclease activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idMG1
Number of Residues1
DetailsMG BINDING SITE.
ChainResidue
AGLU34

Functional Information from PROSITE/UniProt
site_idPS00726
Number of Residues10
DetailsAP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDVIGLQETK
ChainResidueDetails
APRO27-LYS36

site_idPS00727
Number of Residues17
DetailsAP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DTFRHanpqtadrFSWF
ChainResidueDetails
AASP197-PHE213

site_idPS00728
Number of Residues12
DetailsAP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NrGlRIDLlLaS
ChainResidueDetails
AASN223-SER234

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ATYR109

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250
ChainResidueDetails
AASP151

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AASN153
AASP258
AGLU34
AASP151

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250
ChainResidueDetails
AASN153

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Important for catalytic activity => ECO:0000250
ChainResidueDetails
AASP229

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Interaction with DNA substrate => ECO:0000250
ChainResidueDetails
AHIS259

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 160
ChainResidueDetails
AASN7activator, electrostatic stabiliser, hydrogen bond donor
AGLU34metal ligand
AASP151hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor
AASN153activator, electrostatic stabiliser, hydrogen bond donor, metal ligand
AASP229activator, electrostatic stabiliser, hydrogen bond acceptor
AASP258metal ligand
AHIS259hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

218500

PDB entries from 2024-04-17

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