9N5P: PDB entry 9N5P

Crystal structure of human IGG2 fc fragment-fc-gamma receptor iia complex H131 variant. Determined by X-ray diffraction at 2.01 Å resolution. Released 3 Dec 2025.

Method: X-ray diffraction
Resolution: 2.01 Å
Organism: Homo sapiens
Chains: 3
Atoms: 5,280
Mol. weight: 73.52 kDa
Ligands: NAG
Released: 3 Dec 2025

Explore 9N5P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9N5P contains 30 α-helices and 61 β-strands across 3 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: 11 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	239-243	5	1
α-helix	244-246	3
α-helix	247-251	5
β-strand	258-266	9	1
β-strand	274-279	6	2
β-strand	282-284	3	2
β-strand	288-289	2	1
α-helix	290-292	3
β-strand	293-294	2	1
β-strand	300-307	8	1
α-helix	310-314	5
β-strand	319-324	6	2
β-strand	332-336	5	2
α-helix	338-340	3
β-strand	344	1	3
α-helix	345-346	2
β-strand	347-351	5	4
α-helix	352-354	3
α-helix	355-359	5
β-strand	362-372	11	4
β-strand	373	1	3
β-strand	378-383	6	5
β-strand	386-388	3	5
β-strand	391-393	3	4
α-helix	394-396	3
β-strand	397-398	2	4
β-strand	404-413	10	4
α-helix	414-418	5
β-strand	423-428	6	5
α-helix	433-435	3
β-strand	436-441	6	5

Chain B: 11 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	239-243	5	6
α-helix	244-246	3
α-helix	247-251	5
β-strand	258-266	9	6
β-strand	274-279	6	7
β-strand	282-284	3	7
β-strand	288-289	2	6
α-helix	290-292	3
β-strand	293-294	2	6
β-strand	300-307	8	6
α-helix	310-315	6
β-strand	319-324	6	7
β-strand	332-336	5	7
α-helix	338-340	3
β-strand	344	1	8
α-helix	345-346	2
β-strand	347-351	5	9
α-helix	352-354	3
α-helix	355-359	5
β-strand	362-372	11	9
β-strand	373	1	8
β-strand	378-383	6	10
β-strand	386-388	3	10
β-strand	391-393	3	9
α-helix	394-396	3
β-strand	397-398	2	9
β-strand	404-413	10	9
α-helix	414-418	5
β-strand	423-428	6	10
α-helix	433-435	3
β-strand	437-441	5	10

Chain C: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	4	1	11
α-helix	5	1
β-strand	8-10	3	12
β-strand	15-17	3	13
β-strand	21-25	5	12
β-strand	38-41	4	14
β-strand	44-45	2	14
β-strand	53-57	5	12
α-helix	60-62	3
β-strand	64-69	6	14
β-strand	74	1	11
α-helix	75-78	4
β-strand	79-81	3	14
β-strand	82-84	3	13
β-strand	88-91	4	15
β-strand	96-98	3	16
α-helix	101-102	2
β-strand	103-109	7	15
α-helix	110-112	3
β-strand	116-122	7	17
β-strand	125-130	6	17
β-strand	135-138	4	15
α-helix	143-145	3
β-strand	147-155	9	17
β-strand	158-161	4	17
α-helix	162-164	3
β-strand	165-167	3	17
β-strand	168-170	3	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Isoform 1 of Immunoglobulin heavy constant gamma 2	A, B	protein	223	Homo sapiens	Q6N093 (AlphaFold model)
Low affinity immunoglobulin gamma Fc region receptor II-a H131 variant	C	protein	173	Homo sapiens	P12318 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>9N5P_1 Isoform 1 of Immunoglobulin heavy constant gamma 2 (chains A, B)
VECPPCPAPPVAGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVQFNWYVDGVEV
HNAKTKPREEQFNSTFRVVSVLTVVHQDWLNGKEYKCKVSNKGLPAPIEKTISKTKGQPR
EPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPMLDSDGSF
FLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK

Sequence of entity 2 (C), FASTA

>9N5P_2 Low affinity immunoglobulin gamma Fc region receptor II-a H131 variant (chains C)
APPKAVLKLEPPWINVLQEDSVTLTCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANN
NDSGEYTCQTGQTSLSDPVHLTVLSEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTF
FQNGKSQKFSHLDPTFSIPQANHSHSGDYHCTGNIGYTLFSSKPVTITVQVPS

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

Primary citation

Cross-species analysis of Fc gamma RIIa/b (CD32a/b) polymorphisms at position 131: structural and functional insights into the mechanism of IgG- mediated phagocytosis in human and macaque. Tolbert, W.D., Nhan, P.B., Conley, H.E. et al. Front Immunol (2025) 16:1726068-1726068. DOI 10.3389/fimmu.2025.1726068 · PubMed

Other PDB entries of the same protein (UniProt Q6N093 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2HFG 2.61 Å, Crystal structure of hBR3 bound to CB3s-Fab

Browse structure collections

About this viewer

MolViewer shows 9N5P directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.