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1WEF

Catalytic Domain Of Muty From Escherichia Coli K20A Mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0019104molecular_functionDNA N-glycosylase activity
A0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 A 300
ChainResidue
ACYS148
ACYS192
ACYS199
ACYS202
AGLN205
ACYS208
AALA211

Functional Information from PROSITE/UniProt
site_idPS00764
Number of Residues17
DetailsENDONUCLEASE_III_1 Endonuclease III iron-sulfur binding region signature. CtrsKPKCslCplqngC
ChainResidueDetails
ACYS192-CYS208

site_idPS01155
Number of Residues30
DetailsENDONUCLEASE_III_2 Endonuclease III family signature. GkFPetfeeVaa.LPGVGrstAgaiLslSLG
ChainResidueDetails
AGLY102-GLY131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P83847","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P83847","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2abk
ChainResidueDetails
AASP138
ASER120

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2abk
ChainResidueDetails
AASP138
AGLU37

240291

PDB entries from 2025-08-13

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