5NQZ: PDB entry 5NQZ

Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 309. Determined by X-ray diffraction at 1.63 Å resolution. Released 28 Feb 2018.

Method: X-ray diffraction
Resolution: 1.63 Å
Organisms: Neisseria meningitidis MC58, Neisseria meningitidis serogroup C
Chains: 2
Atoms: 4,631
Mol. weight: 59.38 kDa
Ligands: ZN
Released: 28 Feb 2018

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

Secondary structure: helices and β-sheets

5NQZ contains 20 α-helices and 38 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: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	81-86	6
α-helix	87-89	3
α-helix	94	1
α-helix	96	1
β-strand	99-100	2	1
β-strand	109-115	7	2
β-strand	118-122	5	2
β-strand	127-128	2	1
α-helix	130-132	3
α-helix	134	1
β-strand	138-149	12	2
β-strand	152-165	14	2
β-strand	169-180	12	2
β-strand	188-201	14	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	271-279	9	3
β-strand	282-292	11	3
β-strand	298-308B	13	3
β-strand	308K-320	14	3
α-helix	321-322	2

Chain B: 10 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	81-86	6
α-helix	87-89	3
α-helix	94	1
α-helix	96	1
β-strand	99-100	2	5
β-strand	110-115	6	6
β-strand	118-122	5	6
β-strand	127-128	2	5
α-helix	130-132	3
α-helix	134	1
β-strand	138-149	12	6
β-strand	152-165	14	6
β-strand	169-180	12	6
β-strand	188-201	14	6
β-strand	203	1	7
α-helix	204	1
β-strand	205	1	8
α-helix	206-208	3
β-strand	214-223	10	7
β-strand	226-236	11	7
β-strand	241-247	7	7
α-helix	252-254	3
β-strand	257-265	9	7
β-strand	270	1	8
β-strand	271-279	9	7
β-strand	282-292	11	7
β-strand	298-308B	13	7
β-strand	308K-320	14	7
α-helix	321-322	2

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	protein	269	Neisseria meningitidis MC58, Neisseria meningitidis serogroup C	P13415 (AlphaFold model), Q9JXV4 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5NQZ_1 Factor H binding protein,Major outer membrane protein P.IA,Factor H binding protein (chains A, B)
MVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTG
KLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAK
RQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKS
PELNVDLAAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGGKAQEVAGSAEVKTVYYT
KDTNNNLTLVGIRHIGLAAKQLEHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	9

Water and common crystallization additives (EDO, ACT) are not listed.

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:

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.
5NQX 3.66 Å, Structure of a fHbp(V1.1):PorA(P1.16) chimera. Fusion at fHbp position 294.

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