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1WEI

Catalytic Domain Of Muty From Escherichia Coli K20A 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 Residues6
DetailsBINDING SITE FOR RESIDUE ADE A 1428
ChainResidue
AGLU37
AVAL45
AGLN182
AMET185
AHOH530
AEDO1271

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1269
ChainResidue
AALA68
AGLY79
ALEU80
AHOH520
AARG58
AASP64
AASN67

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1270
ChainResidue
AALA150
ASER152
AGLU169
ATHR172
ATYR219
AHOH319

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 1271
ChainResidue
AGLU37
ASER120
ATHR121
AASP138
AMET185
AHOH369
AHOH559
AADE1428

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SF4 A 300
ChainResidue
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
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
AASP138

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

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PDB entries from 2024-11-06

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