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MutM encountering an intrahelical 8-oxoguanine (oxoG) lesion in EC3-loop deletion complex External Resource: Annotation Domain Annotation: SCOP2 Classification SCOP2 Database Homepage Chains Type Family Name Domain Identifier Family Identifier Provenance Source (Version) A SCOP2B Superfamily S13-like H2TH domain 8056364 3000053 SCOP2B (2022-06-29) A SCOP2B Superfamily Glucocorticoid receptor-like (DNA-binding domain) 8056365 3000068 SCOP2B (2022-06-29) A SCOP2B Superfamily FPG N-terminal domain-like 8056363 3000074 SCOP2B (2022-06-29)
Chains Family Name Domain Identifier Architecture Possible Homology Homology Topology Family Provenance Source (Version) A PF01149 e3go8A1 A: beta barrels X: MutM N-terminal domain-like H: N-terminal domain of MutM-like DNA repair proteins (From Topology) T: N-terminal domain of MutM-like DNA repair proteins F: PF01149 ECOD (1.6) A PF06831 e3go8A2 A: alpha arrays X: HhH/H2TH H: H2TH (From Topology) T: H2TH F: PF06831 ECOD (1.6) A PF06827 e3go8A3 A: few secondary structure elements X: Glucocorticoid receptor-like H: C-terminal, Zn-finger domain of MutM-like DNA repair proteins (From Topology) T: C-terminal, Zn-finger domain of MutM-like DNA repair proteins F: PF06827 ECOD (1.6)
Chains Accession Name Description Comments Source PF06827 Zinc finger found in FPG and IleRS (zf-FPG_IleRS) Zinc finger found in FPG and IleRS This zinc binding domain is found at the C-terminus of isoleucyl tRNA synthetase and the enzyme Formamidopyrimidine-DNA glycosylase EC:3.2.2.23. Domain PF01149 Formamidopyrimidine-DNA glycosylase N-terminal domain (Fapy_DNA_glyco) Formamidopyrimidine-DNA glycosylase N-terminal domain Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidised purines from damaged DNA. This family is the N-terminal domain contains eight beta-strands, forming a beta-sandwich with two alpha-helices parallel to its edges [1 ... Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that excises oxidised purines from damaged DNA. This family is the N-terminal domain contains eight beta-strands, forming a beta-sandwich with two alpha-helices parallel to its edges [1]. Less Domain
Chains Polymer Molecular Function Biological Process Cellular Component Formamidopyrimidine-DNA glycosylase - 5'-D(P*GP*GP*TP*AP*GP*AP*TP*CP*CP*GP*GP*AP*CP*G)-3' - - - 5'-D(*GP*CP*GP*TP*CP*CP*(8OG)P*GP*AP*TP*CP*TP*AP*C)-3' - - -