› 1ewi

Solution NMR

HUMAN REPLICATION PROTEIN A: GLOBAL FOLD OF THE N-TERMINAL RPA-70 DOMAIN REVEALS A BASIC CLEFT AND FLEXIBLE C-TERMINAL LINKER

Released:
DOI: 10.2210/pdb1ewi/pdb
PDB entry 1ewi coloured by chain, front view.
PDB entry 1ewi coloured by chain, side view.
PDB entry 1ewi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker.
Jacobs DM, Lipton AS, Isern NG, Daughdrill GW, Lowry DF, Gomes X, Wold MS
J Biomol NMR 14 321-31 (1999)
PMID: 10526407

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151049 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Replication protein A 70 kDa DNA-binding subunit, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 12.49 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P27694 (Residues: 1-114; Coverage: 19%)
Gene names: REPA1, RPA1, RPA70
Sequence domains: Replication factor-A protein 1, N-terminal domain
Structure domains: Nucleic acid-binding proteins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry/simulated annealing

Quick links

Citations

7 review citations

A dynamic model for replication protein A (RPA) function in DNA processing pathways.
Fanning et al. (2006)
6 more

9 mentions without citation

XPA: A key scaffold for human nucleotide excision repair.
Sugitani et al. (2016)
8 more