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1KEA

STRUCTURE OF A THERMOSTABLE THYMINE-DNA GLYCOSYLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000701molecular_functionpurine-specific mismatch base pair DNA N-glycosylase activity
A0003824molecular_functioncatalytic activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006298biological_processmismatch repair
A0006950biological_processresponse to stress
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0032357molecular_functionoxidized purine DNA binding
A0034039molecular_function8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
A0035485molecular_functionadenine/guanine mispair binding
A0046872molecular_functionmetal ion binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0141016molecular_functionG/T mismatch-specific thymine-DNA glycosylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
AHIS31
ACYS66
AGLU68
ACL2001
AACT3004

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 3001
ChainResidue
AGLY124
ALYS125
AACT3002
AHOH5063

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 3002
ChainResidue
ASER14
ATYR164
AACT3001
AHOH5148
AHOH5186

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 3003
ChainResidue
AGLN90
ALYS139
AGLY179
AHOH5133

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 3004
ChainResidue
AGLU68
AARG109
AARG183
AZN1001
ACL2001
AHOH5056
AHOH5191

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 2001
ChainResidue
ACYS66
AGLU68
AZN1001
AACT3004
AHOH5025

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 2002
ChainResidue
AARG33
ATYR36
AVAL110

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SF4 A 300
ChainResidue
ACYS197
ACYS204
ACYS207
AMET209
ASER210
ACYS213
ATYR215

Functional Information from PROSITE/UniProt
site_idPS00764
Number of Residues17
DetailsENDONUCLEASE_III_1 Endonuclease III iron-sulfur binding region signature. CaprKPKCekCgmsklC
ChainResidueDetails
ACYS197-CYS213

site_idPS01155
Number of Residues30
DetailsENDONUCLEASE_III_2 Endonuclease III family signature. GrVPrnrkaIld.LPGVGkytCaavMclAFG
ChainResidueDetails
AGLY108-GLY137

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P83847
ChainResidueDetails
ACYS197
ACYS204
ACYS207
ACYS213

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 2abk
ChainResidueDetails
ATYR126
AASP144

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 2abk
ChainResidueDetails
AGLU42
AASP144

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PDB entries from 2024-12-25

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