6CMG: Hendra Virus Attachment G Glycoprotein

Crystal Structure of the Hendra Virus Attachment G Glycoprotein Bound to a Potent Cross-Reactive Neutralizing Human Monoclonal Antibody m102.3. Determined by X-ray diffraction at 2.7 Å resolution. Released 18 Apr 2018.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: Hendra virus, Homo sapiens
Chains: 3
Atoms: 6,891
Mol. weight: 99.1 kDa
Ligands: NAG
Released: 18 Apr 2018

Explore 6CMG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6CMG contains 14 α-helices and 79 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: 7 helices, 33 β-strands

Element	Residues	Length	Sheet
β-strand	178-179	2	1
α-helix	185-187	3
β-strand	201-202	2	1
β-strand	215-225	11	2
β-strand	228-237	10	2
β-strand	244-257	14	2
β-strand	263-271	9	2
β-strand	279-287	9	3
β-strand	290-297	8	3
α-helix	310-312	3
β-strand	314-320	7	3
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	372-374	3
α-helix	379-381	3
α-helix	394-397	4
β-strand	407-417	11	4
β-strand	425-430	6	4
β-strand	431	1	5
α-helix	432	1
β-strand	442-447	6	6
β-strand	450-455	6	6
β-strand	465-471	7	6
β-strand	475	1	5
β-strand	476-479	4	6
β-strand	509	1	1
β-strand	511-515	5	7
β-strand	520-526	7	7
β-strand	533	1	8
β-strand	535-540	6	7
β-strand	545-550	6	7
β-strand	557	1	8
β-strand	558-568	11	1
β-strand	571-582	12	1
β-strand	587-596	10	1
α-helix	597-598	2

Chain B: 2 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	9
β-strand	12-13	2	10
β-strand	19-25	7	9
α-helix	31-33	3
β-strand	34-39	6	11
β-strand	45-49	5	11
β-strand	55	1	11
β-strand	63-68	6	9
β-strand	71-76	6	9
α-helix	81-83	3
β-strand	86-91	6	11
β-strand	93	1	12
β-strand	97-98	2	11
β-strand	102-103	2	11
β-strand	105-106	2	10
β-strand	111	1	13
β-strand	114-118	5	14
β-strand	129-139	11	14
β-strand	140	1	13
β-strand	145-150	6	15
β-strand	154	1	15
β-strand	159-163	5	14
β-strand	173-182	10	14
β-strand	191-197	7	15
β-strand	205-210	6	15

Chain C: 5 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	16
β-strand	10-12	3	12
β-strand	18-24	7	16
β-strand	33-39	7	12
β-strand	45-52	8	12
β-strand	57-60	4	12
α-helix	62-64	3
β-strand	65	1	16
β-strand	68-73	6	16
β-strand	78-83	6	16
α-helix	88-90	3
β-strand	92-105	14	12
β-strand	112-122	11	12
β-strand	126-130	5	12
α-helix	137-138	2
β-strand	139-143	5	17
β-strand	154-164	11	17
β-strand	170-173	4	18
β-strand	178	1	18
β-strand	182-184	3	17
α-helix	185-187	3
β-strand	188-189	2	17
β-strand	195-204	10	17
α-helix	205-207	3
β-strand	214-218	5	18
β-strand	219	1	19
β-strand	224	1	19
β-strand	227-229	3	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Glycoprotein G	A	protein	428	Hendra virus	O89343 (AlphaFold model)
m102.3 light chain	B	protein	214	Homo sapiens
IgG Heavy chain	C	protein	235	Homo sapiens

Sequence of entity 1 (A), FASTA

>6CMG_1 Glycoprotein G (chains A)
QGVSDLVGLPNQICLQKTTSTILKPRLISYTLPINTREGVCITDPLLAVDNGFFAYSHLE
KIGSCTRGIAKQRIIGVGEVLDRGDKVPSMFMTNVWTPPNPSTIHHCSSTYHEDFYYTLC
AVSHVGDPILNSTSWTESLSLIRLAVRPKSDSGDYNQKYIAITKVERGKYDKVMPYGPSG
IKQGDTLYFPAVGFLPRTEFQYNDSNCPIIHCKYSKAENCRLSMGVNSKSHYILRSGLLK
YNLSLGGDIILQFIEIADNRLTIGSPSKIYNSLGQPVFYQASYSWDTMIKLGDVDTVDPL
RVQWRNNSVISRPGQSQCPRFNVCPEVCWEGTYNDAFLIDRLNWVSAGVYLNSNQTAENP
VFAVFKDNEILYQVPLAEDDTNAQKTITDCFLLENVIWCISLVEIYDTGDSVIRPKLFAV
KIPAQCSE

Sequence of entity 2 (B), FASTA

>6CMG_2 m102.3 light chain (chains B)
EIVMTQSPGTPSLSPGERATLSCRASQSIRSTYLAWYQQKPGQAPRLLIYGASSRATGIP
DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGRSPSFGQGTKVEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKLYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 3 (C), FASTA

>6CMG_3 IgG Heavy chain (chains C)
EVQLVQSGAEVKKRGSSVKVSCKSSGGTFSNYAINWVRQAPGQGLEWMGGIIPILGIANY
AQKFQGRVTITTDESTSTAYMELSSLRSEDTAVYYCARGWGREQLAPHPSQYYYYYYGMD
VWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTS
GVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC

Ligands and cofactors

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

Primary citation

Crystal structure of the Hendra virus attachment G glycoprotein bound to a potent cross-reactive neutralizing human monoclonal antibody. Xu, K., Rockx, B., Xie, Y. et al. PLoS Pathog (2013) 9:e1003684. DOI 10.1371/journal.ppat.1003684 · 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…
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)
8JR3 3.22 Å, Crystal structure of Hendra Virus attachment(G) glycoprotein mutant S586N in complex…
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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