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1J53

Structure of the N-terminal Exonuclease Domain of the Epsilon Subunit of E.coli DNA Polymerase III at pH 8.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0006260biological_processDNA replication
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 3000
ChainResidue
AASP12
AGLU14
AASP167
ATMP2000
AHOH5002

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 3001
ChainResidue
AHOH5146
AASP12
ATMP2000
AHOH5040
AHOH5145

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TMP A 2000
ChainResidue
AASP12
ATHR13
AGLU14
ATHR15
AMET18
AGLU61
AVAL65
AHIS66
APHE102
AHIS162
AASP167
AMN3000
AMN3001
AHOH5002
AHOH5137

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO A 4000
ChainResidue
ATHR123

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 5000
ChainResidue
AARG7
AGLN8
AVAL38
AVAL39

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS162

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AASP12
AGLU14
AGLU61
AHIS66
AASP167

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 11937058
ChainResidueDetails
AGLU61
AGLU14

site_idMCSA1
Number of Residues5
DetailsM-CSA 754
ChainResidueDetails
AASP12metal ligand
AGLU14hydrogen bond acceptor, metal ligand, proton acceptor, proton donor
AGLU61electrostatic stabiliser, increase basicity, polar interaction
AHIS162proton acceptor, proton donor
AASP167metal ligand

221716

PDB entries from 2024-06-26

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