Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1MUD

CATALYTIC DOMAIN OF MUTY FROM ESCHERICHIA COLI, D138N MUTANT COMPLEXED TO ADENINE

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
AARG147
ACYS192
ACYS199
ACYS202
AGLN205
ACYS208
AALA211

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ADE A 301
ChainResidue
AGLN182
AMET185
AHOH1078
AHOH1098
AHOH1147
AGLU37
ALEU40

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ADE A 302
ChainResidue
ATHR193
ASER195
AHOH1072

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 303
ChainResidue
AGLN42
ATHR43
AARG58
AASP64
AALA68
AGLY79
ALEU80
AHOH1111

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
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P83847
ChainResidueDetails
AGLU37

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING:
ChainResidueDetails
ACYS192
ACYS199
ACYS202
ACYS208

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P83847
ChainResidueDetails
AASN138

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 9846876
ChainResidueDetails
AASN138
AGLU37

223166

PDB entries from 2024-07-31

PDB statisticsPDBj update infoContact PDBjnumon