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2ABK

REFINEMENT OF THE NATIVE STRUCTURE OF ENDONUCLEASE III TO A RESOLUTION OF 1.85 ANGSTROM

Replaces:  1ABK
Functional Information from GO Data
ChainGOidnamespacecontents
A0000703molecular_functionoxidized pyrimidine nucleobase lesion DNA N-glycosylase activity
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0004844molecular_functionuracil DNA N-glycosylase activity
A0005515molecular_functionprotein binding
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006285biological_processbase-excision repair, AP site formation
A0006950biological_processresponse to stress
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016829molecular_functionlyase activity
A0019104molecular_functionDNA N-glycosylase activity
A0034644biological_processcellular response to UV
A0046872molecular_functionmetal ion binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
A0097510biological_processbase-excision repair, AP site formation via deaminated base removal
A0140078molecular_functionclass I DNA-(apurinic or apyrimidinic site) endonuclease activity
Functional Information from PDB Data
site_id1
Number of Residues2
DetailsDNA GLYCOSYLASE AND DNA LYASE ACTIVITY
ChainResidue
ALYS120
AASP138

site_id2
Number of Residues1
DetailsDNA BINDING
ChainResidue
ALYS191

site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SF4 A 300
ChainResidue
ACYS203
ATYR205
ATHR148
AHIS182
ACYS187
ACYS194
ACYS197
AGLU200

Functional Information from PROSITE/UniProt
site_idPS00764
Number of Residues17
DetailsENDONUCLEASE_III_1 Endonuclease III iron-sulfur binding region signature. CiarKPRCgsCiiedlC
ChainResidueDetails
ACYS187-CYS203

site_idPS01155
Number of Residues30
DetailsENDONUCLEASE_III_2 Endonuclease III family signature. GeVPedraaLea.LPGVGrktAnvvLntAFG
ChainResidueDetails
AGLY102-GLY131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:7664751, ECO:0007744|PDB:2ABK
ChainResidueDetails
ACYS187
ACYS194
ACYS197
ACYS203

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 1411536, 7664751, 7806489, 10467137, 11695910
ChainResidueDetails
AASP138
ALYS120

site_idMCSA1
Number of Residues2
DetailsM-CSA 888
ChainResidueDetails
ALYS120covalent catalysis
AASP138proton shuttle (general acid/base)

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PDB entries from 2024-09-18

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