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6J44

Crystal structure of the redefined DNA-binding domain of human XPA

Functional Information from GO Data
ChainGOidnamespacecontents
A0003684molecular_functiondamaged DNA binding
A0006289biological_processnucleotide-excision repair
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 301
ChainResidue
ACYS105
ACYS108
ACYS126
ACYS129

Functional Information from PROSITE/UniProt
site_idPS00752
Number of Residues25
DetailsXPA_1 XPA protein signature 1. CeECgkeFm.DsyLmnhFdlptCdnC
ChainResidueDetails
ACYS105-CYS129

site_idPS00753
Number of Residues17
DetailsXPA_2 XPA protein signature 2. LITKTEaKqEYLLkDcD
ChainResidueDetails
ALEU138-ASP154

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsZN_FING: ZN_FING => ECO:0000305|PubMed:2234061, ECO:0000305|PubMed:31253769
ChainResidueDetails
ACYS105-CYS129

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:31253769, ECO:0007744|PDB:1D4U, ECO:0007744|PDB:1XPA, ECO:0007744|PDB:6RO4
ChainResidueDetails
ACYS105
ACYS108
ACYS126
ACYS129

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:16540648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER196

site_idSWS_FT_FI4
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
ChainResidueDetails
ALYS145

227111

PDB entries from 2024-11-06

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