3RY5: Glycosylated fcgammariia

Three-dimensional structure of glycosylated fcgammariia (high-responder polymorphism). Determined by X-ray diffraction at 2.3 Å resolution. Released 31 Aug 2011.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 1
Atoms: 1,435
Mol. weight: 19.15 kDa
Released: 31 Aug 2011

Explore 3RY5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3RY5 contains 8 α-helices and 21 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: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	5-6	2
β-strand	7	1	1
α-helix	8	1
β-strand	9-13	5	2
β-strand	18-20	3	3
β-strand	24-30	7	2
β-strand	41-44	4	4
β-strand	47-48	2	4
β-strand	56-60	5	2
α-helix	63-65	3
β-strand	67-72	6	4
β-strand	77	1	1
α-helix	78-81	4
β-strand	82-84	3	4
β-strand	85-87	3	3
β-strand	91-94	4	5
β-strand	99-100	2	6
α-helix	104-105	2
β-strand	106-112	7	5
α-helix	113-115	3
β-strand	119-125	7	7
β-strand	128-133	6	7
β-strand	138-141	4	5
α-helix	146-148	3
β-strand	150-158	9	7
β-strand	161-164	4	7
α-helix	165-167	3
β-strand	168-170	3	7
β-strand	171-172	2	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Low affinity immunoglobulin gamma fc region receptor II-a	A	protein	170	Homo sapiens	P12318 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3RY5_1 LOW AFFINITY IMMUNOGLOBULIN GAMMA FC REGION RECEPTOR II-A (chains A)
APPKAVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANN
NDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTF
FQNGKSQKFSRLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQ

Primary citation

Structural Basis for Fc{gamma}RIIa Recognition of Human IgG and Formation of Inflammatory Signaling Complexes. Ramsland, P.A., Farrugia, W., Bradford, T.M. et al. J Immunol (2011) 187:3208-3217. DOI 10.4049/jimmunol.1101467 · PubMed

Other PDB entries of the same protein (UniProt P12318 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3RY4 1.5 Å, 1.5 Angstrom resolution structure of glycosylated fcgammariia (low-responder polymorphism)
8CHA 1.81 Å, Fc gamma RIIa 27W/131H variant ectodomain
1FCG 2.0 Å, Ectodomain of human fc gamma receptor, fcgriia
9N5P 2.01 Å, Crystal structure of human IGG2 fc fragment-fc-gamma receptor iia complex H131 variant
9MCX 2.38 Å, Crystal structure of human IgG1 fc fragment-fc-gamma receptor iia complex H131 variant
3D5O 2.8 Å, Structural recognition and functional activation of FcrR by innate pentraxins
1H9V 3.0 Å, Human Fc-gamma-Receptor IIa (FcgRIIa), monoclinic
10FJ 3.5 Å, FcgRIIa in complex with IV.3 Fab
3RY6 3.8 Å, Complex of fcgammariia (CD32) and the FC of human IGG1

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