5EH1: Interferon gamma receptor 2

Crystal structure of the extracellular part of receptor 2 of human interferon gamma. Determined by X-ray diffraction at 1.8 Å resolution. Released 17 Aug 2016.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
1
Atoms
2,121
Mol. weight
27.27 kDa
Ligands
CYS, NAG
Released
17 Aug 2016

Explore 5EH1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5EH1 contains 11 α-helices and 22 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: 11 helices, 22 β-strands

ElementResiduesLengthSheet
β-strand3011
α-helix31-344
β-strand37-4152
β-strand44-4852
α-helix59-613
β-strand62-6873
β-strand75-7623
α-helix79-824
β-strand87-8933
β-strand93-9532
β-strand110-11124
β-strand112-11983
β-strand122-12323
β-strand12411
α-helix125-1262
β-strand127-12823
α-helix129-1313
β-strand132-13324
α-helix134-1374
α-helix1381
β-strand13912
α-helix1401
β-strand144-15185
β-strand154-16075
β-strand171-181116
β-strand187-19266
β-strand196-19945
α-helix202-2032
β-strand207-218126
β-strand224-22636
α-helix227-2326
β-strand233-23646
α-helix237-2382

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Interferon gamma receptor 2Aprotein231Homo sapiensP38484 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5EH1_1 Interferon gamma receptor 2 (chains A)
RSSQLPAPQHPKIRLYNAEQVLSWEPVALSNSTRPVVYQVQFKYTDSKWFTADIMSIGVN
CTQITATECDFTAASPSAGFPMDFNVTLRLRAELGALHSAWVTMPWFQHYRNVTVGPPEN
IEVTPGEGSLIIRFSSPFDIADTSTAFFCYYVHYWEKGGIQQVKGPFRSNSISLDNLKPS
RVYCLQVQAQLLWNKSNIFRVGHLSNISCYETMADASTELQQTGHHHHHHE

Ligands and cofactors

IDNameFormulaCopies
CYSCysteineC3 H7 N O2 S1
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O63

Water and common crystallization additives (GOL) are not listed.

Primary citation

Crystal structure of human interferon-gamma receptor 2 reveals the structural basis for receptor specificity. Mikulecky, P., Zahradnik, J., Kolenko, P. et al. Acta Crystallogr D Struct Biol (2016) 72:1017-1025. DOI 10.1107/S2059798316012237 · PubMed

Other PDB entries of the same protein (UniProt P38484 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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