2JPD: ERCC1 central domain

Solution structure of the ERCC1 central domain. Determined by solution NMR. Released 4 Sept 2007.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
996
Mol. weight
15.46 kDa
Released
4 Sept 2007

Explore 2JPD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2JPD contains 6 α-helices and 6 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: 6 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand101-10331
α-helix105-1073
α-helix111-1155
β-strand121-12331
β-strand130-13341
β-strand136-14271
α-helix143-1486
α-helix151-16313
β-strand166-17271
α-helix179-19214
β-strand195-19951
α-helix202-21514

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DNA excision repair protein ERCC-1Aprotein135Homo sapiensP07992 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2JPD_1 DNA excision repair protein ERCC-1 (chains A)
MAKSNSIIVSPRQRGNPVLKFVRNVPWEFGDVIPDYVLGQSTCALFLSLRYHNLHPDYIH
GRLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLILAWSPEEAGRYLETYKA
YEQKPGGLEHHHHHH

Primary citation

Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization. Tripsianes, K., Folkers, G.E., Zheng, C. et al. Nucleic Acids Res (2007) 35:5789-5798. DOI 10.1093/nar/gkm503 · PubMed

Other PDB entries of the same protein (UniProt P07992 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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