1OVZ: Human FcaRI

Crystal structure of human FcaRI. Determined by X-ray diffraction at 3.0 Å resolution. Released 27 May 2003.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,884
Mol. weight: 48.44 kDa
Ligands: NAG
Released: 27 May 2003

Explore 1OVZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OVZ contains 5 α-helices and 39 β-strands across 2 chains. 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: 3 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	7-9	3
β-strand	10-12	3	1
β-strand	17-19	3	2
β-strand	24-28	5	1
β-strand	36-42	7	3
β-strand	47-49	3	3
β-strand	52-53	2	1
β-strand	63-66	4	1
α-helix	71-73	3
β-strand	75-82	8	3
β-strand	88-90	3	3
β-strand	94-96	3	3
β-strand	97-99	3	2
β-strand	106-109	4	4
β-strand	114-115	2	5
β-strand	122-126	5	4
β-strand	135-139	5	6
β-strand	149-150	2	6
β-strand	156-158	3	4
α-helix	164-166	3
β-strand	168-173	6	6
β-strand	182-183	2	2
β-strand	190-192	3	6
β-strand	193-194	2	5

Chain B: 2 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	10-12	3	7
β-strand	17-19	3	8
β-strand	24-28	5	7
α-helix	29-30	2
β-strand	36-42	7	9
β-strand	47-49	3	9
β-strand	52-54	3	7
β-strand	63-66	4	7
α-helix	71-73	3
β-strand	75-82	8	9
β-strand	88-90	3	9
β-strand	94-96	3	9
β-strand	97-99	3	8
β-strand	107-108	2	10
β-strand	124-125	2	10
β-strand	135-139	5	11
β-strand	149-150	2	11
β-strand	168-173	6	11
β-strand	182	1	8
β-strand	190-192	3	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Immunoglobulin alpha Fc receptor	A, B	protein	207	Homo sapiens	P24071 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1OVZ_1 Immunoglobulin alpha Fc receptor (chains A, B)
QEGDFPMPFISAKSSPVIPLDGSVKIQCQAIREAYLTQLMIIKNSTYREIGRRLKFWNET
DPEFVIDHMDANKAGRYQCQYRIGHYRFRYSDTLELVVTGLYGKPFLSADRGLVLMPGEN
ISLTCSSAHIPFDRFSLAKEGELSLPQHQSGEHPANFSLGPVDLNVSGIYRCYGWYNRSP
YLWSFPSNALELVVTAIDGRAHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3

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

Primary citation

Insights into IgA-mediated immune responses from the crystal structures of human Fc-alpha-RI and its complex with IgA1-Fc. Herr, A.B., Ballister, E.R., Bjorkman, P.J. Nature (2003) 423:614-620. DOI 10.1038/nature01685 · PubMed

Other PDB entries of the same protein (UniProt P24071 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9OFS 1.95 Å, Crystal structure of the human IGA2m2 FC fragment-FC-alpha receptor (CD89) complex
1UCT 2.1 Å, Crystal structure of the extracellular fragment of Fc alpha Receptor I (CD89)
9OV2 2.3 Å, Crystal structure of human IGA2M1 FC fragment-FC-alpha receptor (CD89) complex
9OFR 2.65 Å, Crystal structure of the human IGA1 fc fragment-fc-alpha receptor (CD89) complex
1OW0 3.1 Å, Crystal structure of human FcaRI bound to IgA1-Fc
8SKU 3.2 Å, Structure of human SIgA1 in complex with human CD89 (FcaR1)

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