5NQX: PDB entry 5NQX

Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 294. Determined by X-ray diffraction at 3.66 Å resolution. Released 28 Feb 2018.

Method: X-ray diffraction
Resolution: 3.66 Å
Organisms: Neisseria meningitidis MC58, Neisseria meningitidis serogroup C
Chains: 5
Atoms: 9,572
Mol. weight: 145.92 kDa
Released: 28 Feb 2018

Explore 5NQX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NQX contains 40 α-helices and 107 β-strands across 5 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.

Chains A and E: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	81-86	6
α-helix	88-89	2
β-strand	98-100	3	6
β-strand	109-115	7	7
β-strand	118-122	5	7
α-helix	126	1
β-strand	127-129	3	6
α-helix	130-132	3
α-helix	134	1
β-strand	138-149	12	7
β-strand	152-165	14	7
β-strand	169-180	12	7
β-strand	188-201	14	7
β-strand	203	1	8
α-helix	204	1
β-strand	205	1	9
α-helix	206-208	3
β-strand	214-223	10	8
β-strand	226-236	11	8
β-strand	241-247	7	8
α-helix	252-254	3
β-strand	257-265	9	8
β-strand	270	1	9
β-strand	271-278	8	8
β-strand	283-292	10	8
β-strand	293B-293D	3	10
β-strand	293J-294	4	10
β-strand	298-307	10	8
β-strand	310-319	10	8

Chain B: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	81-86	6
α-helix	88-89	2
β-strand	98-100	3	11
β-strand	109-115	7	12
β-strand	118-122	5	12
α-helix	126	1
β-strand	127-129	3	11
α-helix	130-132	3
α-helix	134	1
β-strand	138-148	11	12
β-strand	153-165	13	12
β-strand	169-179	11	12
β-strand	190-201	12	12
β-strand	203	1	13
α-helix	204	1
β-strand	205	1	14
α-helix	206-208	3
β-strand	214-223	10	13
β-strand	226-236	11	13
β-strand	241-247	7	13
α-helix	252-254	3
β-strand	257-265	9	13
β-strand	270	1	14
β-strand	271-278	8	13
β-strand	283-292	10	13
β-strand	293B-293D	3	7
β-strand	293J-295	5	7
β-strand	298-307	10	13
β-strand	310-319	10	13

Chain C: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	81-86	6
α-helix	88-89	2
β-strand	98-100	3	1
β-strand	109-115	7	2
β-strand	118-122	5	2
α-helix	126	1
β-strand	127-129	3	1
α-helix	130-132	3
α-helix	134	1
β-strand	138-148	11	2
β-strand	153-165	13	2
β-strand	169-179	11	2
β-strand	189-201	13	2
β-strand	203	1	3
α-helix	204	1
β-strand	205	1	4
α-helix	206-208	3
β-strand	214-223	10	3
β-strand	226-236	11	3
β-strand	241-247	7	3
α-helix	252-254	3
β-strand	257-265	9	3
β-strand	270	1	4
β-strand	271-278	8	3
β-strand	283-292	10	3
β-strand	293B-293D	3	5
β-strand	293J-294	4	5
β-strand	298-307	10	3
β-strand	310-319	10	3

Chain D: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	81-86	6
α-helix	88-89	2
β-strand	98-100	3	15
β-strand	109-115	7	16
β-strand	118-122	5	16
α-helix	126	1
β-strand	127-129	3	15
α-helix	130-132	3
α-helix	134	1
β-strand	138-149	12	16
β-strand	152-165	14	16
β-strand	169-180	12	16
β-strand	185	1	17
β-strand	187	1	17
β-strand	188-201	14	16
β-strand	203	1	18
α-helix	204	1
β-strand	205	1	19
α-helix	206-208	3
β-strand	214-223	10	18
β-strand	226-236	11	18
β-strand	241-247	7	18
α-helix	252-254	3
β-strand	257-265	9	18
β-strand	270	1	19
β-strand	271-278	8	18
β-strand	283-292	10	18
β-strand	293B-293D	3	2
β-strand	293J-295	5	2
β-strand	298-307	10	18
β-strand	310-319	10	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Factor H binding protein,Major outer membrane protein P.IA,Factor H binding protein	A, B, C, D, E	protein	269	Neisseria meningitidis MC58, Neisseria meningitidis serogroup C	P13415 (AlphaFold model), Q9JXV4 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>5NQX_1 Factor H binding protein,Major outer membrane protein P.IA,Factor H binding protein (chains A, B, C, D, E)
MVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTG
KLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAK
RQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKS
PELNVDLAAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGYYTKDTNNNLTLVKAQEV
AGSAEVKTVNGIRHIGLAAKQLEHHHHHH

Primary citation

Structure-based design of chimeric antigens for multivalent protein vaccines. Hollingshead, S., Jongerius, I., Exley, R.M. et al. Nat Commun (2018) 9:1051-1051. DOI 10.1038/s41467-018-03146-7 · PubMed

Other PDB entries of the same protein (UniProt P13415 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5NQZ 1.63 Å, Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 309.
5NQY 2.6 Å, Structure of a fHbp(V1.4):PorA(P1.16) chimera. Fusion at fHbp position 309.
5NQP 2.86 Å, Structure of a fHbp(V1.4):PorA(P1.16) chimera. Fusion at fHbp position 151.

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