› 1p97

Solution NMR

NMR structure of the C-terminal PAS domain of HIF2a

Released:
DOI: 10.2210/pdb1p97/pdb
PDB entry 1p97 coloured by chain, ensemble of 20 models, front view.
PDB entry 1p97 coloured by chain, ensemble of 20 models, side view.
PDB entry 1p97 coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for PAS domain heterodimerization in the basic helix--loop--helix-PAS transcription factor hypoxia-inducible factor.
Erbel PJ, Card PB, Karakuzu O, Bruick RK, Gardner KH
Proc Natl Acad Sci U S A 100 15504-9 (2003)
PMID: 14668441

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189272 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endothelial PAS domain-containing protein 1 Chain: A
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 13.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99814 (Residues: 240-350; Coverage: 13%)
Gene names: BHLHE73, EPAS1, HIF2A, MOP2, PASD2
Sequence domains: PAS domain
Structure domains: PAS domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

26 review citations

Exactly the same but different: promiscuity and diversity in the molecular mechanisms of action of the aryl hydrocarbon (dioxin) receptor.
Denison et al. (2011)
25 more

30 mentions without citation

Structure and signaling mechanism of Per-ARNT-Sim domains.
Möglich et al. (2009)
29 more