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7RDT

Structure of human NTHL1 - linker 1 chimera

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0005634cellular_componentnucleus
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006285biological_processbase-excision repair, AP site formation
A0019104molecular_functionDNA N-glycosylase activity
A0051539molecular_function4 iron, 4 sulfur cluster binding
Functional Information from PROSITE/UniProt
site_idPS01155
Number of Residues30
DetailsENDONUCLEASE_III_2 Endonuclease III family signature. GdIPasvaeLva.LPGVGpkmAhlaMavAWG
ChainResidueDetails
AGLY195-GLY224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile; for N-glycosylase activity => ECO:0000255|HAMAP-Rule:MF_03183, ECO:0000269|PubMed:9705289
ChainResidueDetails
ALYS213

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03183
ChainResidueDetails
ACYS283
ACYS290
ACYS293
ACYS299

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for catalytic activity
ChainResidueDetails
AASP232

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER71

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
ASER73

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PDB entries from 2024-07-24

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