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3G8V

The rationally designed catalytically inactive mutant Mth0212(D151N)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0006281biological_processDNA repair
A0008311molecular_functiondouble-stranded DNA 3'-5' DNA exonuclease activity
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0046872molecular_functionmetal ion binding
A0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 266
ChainResidue
AGLU54
AGLY55
ATYR56
AASP242
AHOH295

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 267
ChainResidue
ASER198
AASP199

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE GOL A 268
ChainResidue
AGLU89

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PG4 A 269
ChainResidue
AASP32
AILE33
ATHR75
ALYS76
AVAL77
APHE102
AALA2

Functional Information from PROSITE/UniProt
site_idPS00726
Number of Residues10
DetailsAP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQEIK
ChainResidueDetails
APRO31-LYS40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:20434457
ChainResidueDetails
AASN151

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:20434457, ECO:0000269|Ref.7
ChainResidueDetails
AASN12
AGLU38

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20434457
ChainResidueDetails
AASN151
AASN153
AHIS248

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PDB entries from 2024-07-10

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