1D4U: Nucleotide excision repair protein xpa

Interactions of human nucleotide excision repair protein xpa with RPA70 and DNA: chemical shift mapping and 15N NMR relaxation studies. Determined by solution NMR. Released 17 Oct 1999.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
928
Mol. weight
13.34 kDa
Ligands
ZN
Released
17 Oct 1999

Explore 1D4U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1D4U contains 4 α-helices and 5 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand6-721
β-strand14-1521
β-strand42-4322
α-helix441
α-helix45-495
β-strand67-6932
β-strand82-8432
α-helix86-9611
α-helix100-10910

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Nucleotide excision repair protein xpa (xpa-mbd)Aprotein111Homo sapiensP23025 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1D4U_1 NUCLEOTIDE EXCISION REPAIR PROTEIN XPA (XPA-MBD) (chains A)
MEFDYVICEECGKEFMDSYLMDHFDLPTCDDCRDADDKHKLITKTEAKQEYLLKDCDLEK
REPPLKFIVKKNPHHSQWGDMKLYLKLQIVKRSLEVWGSQEALEEAKEVRQ

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Primary citation

Interactions of human nucleotide excision repair protein XPA with DNA and RPA70 Delta C327: chemical shift mapping and 15N NMR relaxation studies. Buchko, G.W., Daughdrill, G.W., de Lorimier, R. et al. Biochemistry (1999) 38:15116-15128. DOI 10.1021/bi991755p · PubMed

Other PDB entries of the same protein (UniProt P23025 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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