› 1qp9

X-ray diffraction
2.8Å resolution

STRUCTURE OF HAP1-PC7 COMPLEXED TO THE UAS OF CYC7

Released:
DOI: 10.2210/pdb1qp9/pdb
PDB entry 1qp9 coloured by chain, front view.
PDB entry 1qp9 coloured by chain, side view.
PDB entry 1qp9 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of HAP1-PC7 bound to DNA: implications for DNA recognition and allosteric effects of DNA-binding on transcriptional activation.
Lukens AK, King DA, Marmorstein R
Nucleic Acids Res 28 3853-63 (2000)
PMID: 11024163

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-114456 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Heme-responsive zinc finger transcription factor HAP1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 76 amino acids
Theoretical weight: 9.09 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CS82 (Residues: 55-130; Coverage: 5%)
Gene names: CYP1, HAP1
Sequence domains: Fungal Zn(2)-Cys(6) binuclear cluster domain
Structure domains:
DNA (5'-D(*AP*CP*GP*CP*TP*AP*TP*TP*AP*TP*CP*GP*CP*TP*AP*TP*TP*AP*GP*T)-3') Chains: E, G
Molecule details ›
Chains: E, G
Length: 20 nucleotides
Theoretical weight: 6.1 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
DNA (5'-D(*AP*CP*TP*AP*AP*TP*AP*GP*CP*GP*AP*TP*AP*AP*TP*AP*GP*CP*GP*T)-3') Chains: F, H
Molecule details ›
Chains: F, H
Length: 20 nucleotides
Theoretical weight: 6.17 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand ZN 9 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 85.9Å b: 90.9Å c: 96.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.255 0.255 0.294
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

The different (sur)faces of Rap1p.
Piña et al. (2003)
6 other articles

5 mentions without citation

How sequence directs bending in tropomyosin and other two-stranded alpha-helical coiled coils.
Brown JH. (2010)
4 more