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5A39

Structure of Rad14 in complex with cisplatin containing DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003684molecular_functiondamaged DNA binding
A0006289biological_processnucleotide-excision repair
B0003684molecular_functiondamaged DNA binding
B0006289biological_processnucleotide-excision repair
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 300
ChainResidue
ACYS103
ACYS106
ACYS125
ACYS128

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 300
ChainResidue
BCYS103
BCYS106
BCYS125
BCYS128

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CPT C 1015
ChainResidue
CDG8
CDG9
CDT10
CCPT1016
CDC7

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CPT C 1016
ChainResidue
CDC7
CDG8
CCPT1015

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CPT D 1015
ChainResidue
DCPT1016
GDC6
GDG7

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CPT D 1016
ChainResidue
DCPT1015
GDA4
GDC5
GDC6
GDG7

Functional Information from PROSITE/UniProt
site_idPS00752
Number of Residues26
DetailsXPA_1 XPA protein signature 1. CiEChinIemDpvLhdvFklqvCkqC
ChainResidueDetails
ACYS103-CYS128

site_idPS00753
Number of Residues17
DetailsXPA_2 XPA protein signature 2. LLTKTEcKeDYFLtDpE
ChainResidueDetails
ALEU138-GLU154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues50
DetailsZN_FING: ZN_FING => ECO:0000305|PubMed:26100901
ChainResidueDetails
ACYS103-CYS128
BCYS103-CYS128

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:26100901
ChainResidueDetails
ACYS103
ACYS106
ACYS125
ACYS128
BCYS103
BCYS106
BCYS125
BCYS128

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PDB entries from 2024-07-24

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