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6TUR

human XPG, Apo1 form

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0003677molecular_functionDNA binding
AAA0003697molecular_functionsingle-stranded DNA binding
AAA0003824molecular_functioncatalytic activity
AAA0004518molecular_functionnuclease activity
AAA0004519molecular_functionendonuclease activity
AAA0005634cellular_componentnucleus
AAA0006289biological_processnucleotide-excision repair
AAA0016788molecular_functionhydrolase activity, acting on ester bonds
BBB0003677molecular_functionDNA binding
BBB0003697molecular_functionsingle-stranded DNA binding
BBB0003824molecular_functioncatalytic activity
BBB0004518molecular_functionnuclease activity
BBB0004519molecular_functionendonuclease activity
BBB0005634cellular_componentnucleus
BBB0006289biological_processnucleotide-excision repair
BBB0016788molecular_functionhydrolase activity, acting on ester bonds
CCC0003677molecular_functionDNA binding
CCC0003697molecular_functionsingle-stranded DNA binding
CCC0003824molecular_functioncatalytic activity
CCC0004518molecular_functionnuclease activity
CCC0004519molecular_functionendonuclease activity
CCC0005634cellular_componentnucleus
CCC0006289biological_processnucleotide-excision repair
CCC0016788molecular_functionhydrolase activity, acting on ester bonds
DDD0003677molecular_functionDNA binding
DDD0003697molecular_functionsingle-stranded DNA binding
DDD0003824molecular_functioncatalytic activity
DDD0004518molecular_functionnuclease activity
DDD0004519molecular_functionendonuclease activity
DDD0005634cellular_componentnucleus
DDD0006289biological_processnucleotide-excision repair
DDD0016788molecular_functionhydrolase activity, acting on ester bonds
Functional Information from PROSITE/UniProt
site_idPS00841
Number of Residues15
DetailsXPG_1 XPG protein signature 1. IRPiFVFDGdaPlLK
ChainResidueDetails
AAAILE70-LYS84

site_idPS00842
Number of Residues15
DetailsXPG_2 XPG protein signature 2. GIPYIqAPmEAEAQC
ChainResidueDetails
AAAGLY780-CYS794

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues28
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P39748
ChainResidueDetails
CCCGLU789
CCCGLU791
CCCASP810
CCCALA812
CCCASP861
DDDASP30
DDDASP77
DDDGLU789
DDDGLU791
DDDASP810
DDDALA812
DDDASP861
AAAASP810
AAAALA812
AAAASP861
BBBASP30
BBBASP77
BBBGLU789
BBBGLU791
BBBASP810
BBBALA812
BBBASP861
CCCASP30
CCCASP77
AAAASP30
AAAASP77
AAAGLU789
AAAGLU791

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
DDDLYS8
AAALYS8
BBBLYS8
CCCLYS8

site_idSWS_FT_FI3
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P35689
ChainResidueDetails

221051

PDB entries from 2024-06-12

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