8JR3: Glycoprotein G

Crystal structure of Hendra Virus attachment(G) glycoprotein mutant S586N in complex with neutralizing antibody 14F8. Determined by X-ray diffraction at 3.22 Å resolution. Released 19 Jun 2024.

Method: X-ray diffraction
Resolution: 3.22 Å
Organisms: Hendra virus (isolate Horse/Autralia/Hendra/1994), Mus musculus
Chains: 6
Atoms: 13,414
Mol. weight: 191.27 kDa
Ligands: NAG
Released: 19 Jun 2024

Explore 8JR3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8JR3 contains 34 α-helices and 145 β-strands across 6 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: 5 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	16
β-strand	11-12	2	17
β-strand	18-25	8	16
β-strand	33-39	7	18
β-strand	46-51	6	18
β-strand	57-59	3	18
α-helix	61-63	3
β-strand	67-72	6	16
β-strand	77-82	6	16
α-helix	87-89	3
β-strand	91-99	9	18
β-strand	102-106	5	18
β-strand	110-112	3	18
β-strand	113-114	2	17
α-helix	118-119	2
α-helix	121-122	2
β-strand	123-127	5	19
β-strand	138-148	11	19
β-strand	154-157	4	20
β-strand	162	1	20
β-strand	166-168	3	19
α-helix	169-171	3
β-strand	172-173	2	19
β-strand	179-188	10	19
β-strand	192	1	21
β-strand	195	1	21
β-strand	198-203	6	20
β-strand	208-213	6	20

Chain B: 7 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	26
β-strand	11-12	2	27
β-strand	16-25	10	26
β-strand	34-39	6	28
α-helix	44-45	2
β-strand	46-51	6	28
β-strand	57-59	3	28
α-helix	61-63	3
β-strand	67-72	6	26
β-strand	77-85	9	26
α-helix	87-89	3
β-strand	91-98	8	28
β-strand	103-106	4	28
β-strand	110-112	3	28
β-strand	113-114	2	27
α-helix	118-119	2
α-helix	121-122	2
β-strand	123-127	5	29
α-helix	128-130	3
β-strand	138-148	11	29
β-strand	154-157	4	30
β-strand	162	1	30
β-strand	166-168	3	29
α-helix	169-171	3
β-strand	172-173	2	29
β-strand	179-188	10	29
β-strand	198-203	6	30
β-strand	208-213	6	30

Chain C: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	31
β-strand	10-14	5	32
β-strand	18-25	8	31
β-strand	30	1	33
β-strand	36	1	33
β-strand	38-43	6	32
β-strand	50-54	5	32
β-strand	58-59	2	32
α-helix	60	1
β-strand	67-72	6	31
β-strand	75-81	7	31
α-helix	85-87	3
β-strand	90-95	6	32
β-strand	102-103	2	32
β-strand	107-112	6	32
β-strand	119-123	5	34
α-helix	124-126	3
α-helix	127-132	6
β-strand	134-144	11	34
β-strand	150-155	6	35
β-strand	159	1	35
β-strand	164-168	5	34
α-helix	169-172	4
β-strand	178-187	10	34
α-helix	188-193	6
β-strand	197-202	6	35
β-strand	210-211	2	35

Chain D: 6 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	22
β-strand	10-14	5	23
β-strand	19-25	7	22
β-strand	38-43	6	23
β-strand	50-54	5	23
β-strand	58-59	2	23
α-helix	60	1
β-strand	67-72	6	22
β-strand	75-80	6	22
α-helix	85-87	3
β-strand	89-95	7	23
β-strand	102-103	2	23
β-strand	108-112	5	23
β-strand	119-123	5	24
α-helix	124-126	3
α-helix	127-132	6
β-strand	134-144	11	24
β-strand	150-155	6	25
β-strand	158-159	2	25
β-strand	165-168	4	24
α-helix	169-172	4
β-strand	178-187	10	24
α-helix	188-193	6
β-strand	197-202	6	25
β-strand	210-211	2	25

Chain E: 5 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	200-202	3	1
α-helix	204-206	3
β-strand	216-225	10	2
β-strand	228-238	11	2
β-strand	243-257	15	2
β-strand	263-271	9	2
β-strand	279-287	9	3
β-strand	290-297	8	3
β-strand	314-320	7	3
α-helix	323-324	2
β-strand	332-337	6	3
β-strand	339-341	3	4
β-strand	347-350	4	4
β-strand	354	1	3
β-strand	356-358	3	4
β-strand	361-371	11	4
α-helix	379-381	3
α-helix	394-397	4
β-strand	407-417	11	4
β-strand	425-430	6	4
α-helix	431-432	2
β-strand	442-447	6	5
β-strand	450-455	6	5
β-strand	465-468	4	5
β-strand	469-471	3	6
β-strand	476-477	2	6
β-strand	509	1	1
β-strand	511-515	5	7
β-strand	520-526	7	7
β-strand	535-541	7	7
β-strand	544-550	7	7
β-strand	558-568	11	1
β-strand	571-582	12	1
β-strand	587-596	10	1

Chain F: 5 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	201-202	2	8
α-helix	204-206	3
β-strand	216-225	10	9
β-strand	228-237	10	9
β-strand	244-257	14	9
β-strand	263-271	9	9
β-strand	279-287	9	10
β-strand	290-297	8	10
β-strand	314-320	7	10
β-strand	332-337	6	10
β-strand	339-341	3	11
β-strand	347-350	4	11
β-strand	354	1	10
β-strand	356-358	3	11
β-strand	361-371	11	11
α-helix	379-381	3
α-helix	394-397	4
β-strand	407-417	11	11
β-strand	425-430	6	11
α-helix	431-432	2
β-strand	442-447	6	12
β-strand	450-455	6	12
β-strand	463	1	13
β-strand	465-471	7	12
β-strand	476-479	4	12
β-strand	486	1	13
β-strand	509	1	8
β-strand	511-515	5	14
β-strand	520-526	7	14
β-strand	533	1	15
β-strand	535-540	6	14
β-strand	545-550	6	14
β-strand	557	1	15
β-strand	558-568	11	8
β-strand	571-582	12	8
β-strand	587-596	10	8
α-helix	597-598	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glycoprotein G	E, F	protein	416	Hendra virus (isolate Horse/Autralia/Hendra/1994)	O89343 (AlphaFold model)
Heavy chain of neutralizing antibody 14F8	A, B	protein	217	Mus musculus
Light chain of neutralizing antibody 14F8	C, D	protein	212	Mus musculus

Sequence of entity 1 (E, F), FASTA

>8JR3_1 Glycoprotein G (chains E, F)
ICLQKTTSTILKPRLISYTLPINTREGVCITDPLLAVDNGFFAYSHLEKIGSCTRGIAKQ
RIIGVGEVLDRGDKVPSMFMTNVWTPPNPSTIHHCSSTYHEDFYYTLCAVSHVGDPILNS
TSWTESLSLIRLAVRPKSDSGDYNQKYIAITKVERGKYDKVMPYGPSGIKQGDTLYFPAV
GFLPRTEFQYNDSNCPIIHCKYSKAENCRLSMGVNSKSHYILRSGLLKYNLSLGGDIILQ
FIEIADNRLTIGSPSKIYNSLGQPVFYQASYSWDTMIKLGDVDTVDPLRVQWRNNSVISR
PGQSQCPRFNVCPEVCWEGTYNDAFLIDRLNWVSAGVYLNSNQTAENPVFAVFKDNEILY
QVPLAEDDTNAQKTITDCFLLENVIWCISLVEIYDTGDNVIRPKLFAVKIPAQCSE

Sequence of entity 2 (A, B), FASTA

>8JR3_2 Heavy chain of neutralizing antibody 14F8 (chains A, B)
QVQLKESGPGLVAPSQSLSITCTVSGFSLTSYDISWIRQPPGKGLEWLGVIWTGGVTNYN
SAFLSRLSISKDNSKSQVFLKMNSLQTDDTAIYYCVREGDWFFDVWGAGTTVTVSSASTK
GPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYS
LSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK

Sequence of entity 3 (C, D), FASTA

>8JR3_3 Light chain of neutralizing antibody 14F8 (chains C, D)
DVLMTQTPLSLPVSLGDQASISCRSSQSIVHSNGNTYLEWYLQKPGQSPQLLIYKVSNRF
SGVPDRFSGSGSGTDFTLKINRVEAEDLGLYYCFQASHVPYTFGGGTKLEIKRTVAAPSV
FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL
SSTLTLSKADYEKHKLYACEVTHQGLSSPVTK

Ligands and cofactors

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

Primary citation

Single amino acid substitution in Hendra virus attachment glycoprotein induces cross-neutralizing antibodies against Nipah virus. Li, Y., Huang, X., Li, R. et al. Signal Transduct Target Ther (2025) 10:276-276. DOI 10.1038/s41392-025-02370-0 · PubMed

Other PDB entries of the same protein (UniProt O89343 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6VY4 2.0 Å, Crystal structure of Hendra receptor binding protein head domain in complex with human…
6PD4 2.2 Å, Crystal Structure of Hendra Virus Attachment G Glycoprotein
6VY6 2.6 Å, Crystal structure of Hendra receptor binding protein head domain in complex with human…
6CMG 2.7 Å, Crystal Structure of the Hendra Virus Attachment G Glycoprotein Bound to a Potent…
6PDL 2.7 Å, Crystal Structure of Hendra Virus Attachment G Glycoprotein in Complex with Receptor…
6CMI 2.72 Å, Crystal Structure of the Hendra Virus Attachment G Glycoprotein Bound to a Potent…
7SYY 2.74 Å, Hendra virus G protein head domain in complex with cross-neutralizing murine antibody…
7SYZ 2.86 Å, Hendra virus G protein head domain in complex with cross-neutralizing murine antibody…
2X9M 2.9 Å, Hendra virus attachment glycoprotein
8VF1 3.0 Å, Crystal Structure of the Hendra Virus Attachment G glycoprotein (HeV-G)
2VSK 3.3 Å, Hendra virus attachment glycoprotein in complex with human cell surface receptor ephrinB2
8JR5 3.3 Å, Crystal structure of Hendra Virus attachment(G) glycoprotein mutant S586N

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