Oxyhemoglobin, R state
Human hemoglobin in the oxygen-bound R state. The classic structure that captures cooperative binding mid-cycle.
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Classic 129-residue enzyme that cleaves bacterial cell walls. A long-standing benchmark for force-field validation and protein dynamics.
Human hemoglobin in the oxygen-bound R state. The classic structure that captures cooperative binding mid-cycle.
Closed-trimer prefusion conformation of the spike glycoprotein. The starting state for receptor-binding-domain opening dynamics.
Cas9 bound to a single-guide RNA and target DNA. The complete editing complex in a cleavage-ready geometry.
β2 adrenergic receptor captured coupled to its heterotrimeric Gs partner. A landmark GPCR signaling complex.
Twelve base pairs of canonical B-form DNA — the dodecamer that defined our picture of double-helix geometry.
The first protein structure ever solved by X-ray crystallography (Kendrew, 1958). Still a benchmark for oxygen-storage dynamics.
Human deoxyhemoglobin in the tense T state. Pairs naturally with 1HHO to study the allosteric switch behind cooperative oxygen binding.
Bovine rhodopsin in its dark resting state. A cornerstone for visual-pigment activation dynamics.
One of the few full-length immunoglobulin structures available — hinges, Fab arms, and Fc all resolved.
Src tyrosine kinase in its closed, autoinhibited conformation — the regulatory baseline that activation has to overcome.
PKA catalytic subunit bound to ATP and substrate peptide — the textbook reference structure for protein kinases.
A tetrameric water channel embedded in a plant plasma membrane. Each monomer gates water flow through a narrow selectivity filter.
147 base pairs of DNA wrapped around a histone octamer (two copies of H2A, H2B, H3, H4). The fundamental unit of chromatin.
Small, exceptionally stable Kunitz-domain inhibitor of serine proteases — one of the most thoroughly studied proteins in biophysics.