2YPV

Crystal structure of the Meningococcal vaccine antigen factor H binding protein in complex with a bactericidal antibody

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
IMGT Antibody Annotation
SAbDab Antibody Annotation
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B [auth H]	d2ypvh1	All beta proteins	Immunoglobulin-like beta-sandwich	Immunoglobulin	V set domains (antibody variable domain-like)	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B [auth H]	d2ypvh2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
C [auth L]	d2ypvl2	All beta proteins	Immunoglobulin-like beta-sandwich	Immunoglobulin	C1 set domains (antibody constant domain-like)	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
C [auth L]	d2ypvl1	All beta proteins	Immunoglobulin-like beta-sandwich	Immunoglobulin	automated matches	automated matches	(Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Lipoprot_C_1st	e2ypvA1	A: beta barrels	X: Outer membrane meander beta-barrels	H: OMPA-like (From Topology)	T: OMPA-like	F: Lipoprot_C_1st	ECOD (1.6)
A	Lipoprot_C_2nd	e2ypvA2	A: beta barrels	X: Factor H-binding protein (fHbp) N-terminal beta-barrel domain (From Topology)	H: Factor H-binding protein (fHbp) N-terminal beta-barrel domain (From Topology)	T: Factor H-binding protein (fHbp) N-terminal beta-barrel domain	F: Lipoprot_C_2nd	ECOD (1.6)
B [auth H]	V-set_8	e2ypvH1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: V-set_8	ECOD (1.6)
B [auth H]	C1-set_1	e2ypvH2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: C1-set_1	ECOD (1.6)
C [auth L]	C1-set_4	e2ypvL2	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: C1-set_4	ECOD (1.6)
C [auth L]	V-set	e2ypvL1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: V-set	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.1980	Mainly Beta	Sandwich	Immunoglobulin-like		CATH (4.3.0)
A	2.40.160.90	Mainly Beta	Beta Barrel	Porin		CATH (4.3.0)
B [auth H]	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)
C [auth L]	2.60.40.10	Mainly Beta	Sandwich	Immunoglobulin-like	Immunoglobulins	CATH (4.3.0)

IMGT Antibody Annotation IMGT Database Homepage

Chain	Protein Name	Description	Organism Name	Gene Allele Name(s)	Domain Name(s)	Receptor Type	Receptor Description	Provenance Source
B [auth H]	Fab 12C1	VH-CH1	Mus musculus (house mouse)	IGHV1-3901, IGHJ201, IGHG2B*02	V-DOMAIN VH, C-DOMAIN CH1	IG	FAB-GAMMA-2B_KAPPA	IMGT (202449-0)
C [auth L]	Fab 12C1	L-KAPPA	Mus musculus (house mouse)	IGKV14-11101, IGKJ101, IGKJ102, IGKJ201, IGKC01, IGKC02	V-DOMAIN V-KAPPA, C-DOMAIN C-KAPPA	IG	FAB-GAMMA-2B_KAPPA	IMGT (202449-0)

SAbDab Antibody Annotation SAbDab Database Homepage

Chain	Chain Class	Chain Subclass	Chain Type	Antigen Name(s)	Provenance Source
B [auth H]	Heavy Chain	IGHV1	-	lipoprotein	SAbDab (2024-12-13)
C [auth L]	Light Chain	IGKV14	Kappa	lipoprotein	SAbDab (2024-12-13)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF08794	Factor H binding protein, C-terminal (FHBP_C)	Factor H binding protein, C-terminal	Factor H binding protein (also known as GNA1870) is a surface exposed lipoprotein in Neisseria meningitidis that is a potent antigen and a potential candidate for a vaccine against meningococcal disease [1-4]. The structure of the C-terminal domain c ...	Factor H binding protein (also known as GNA1870) is a surface exposed lipoprotein in Neisseria meningitidis that is a potent antigen and a potential candidate for a vaccine against meningococcal disease [1-4]. The structure of the C-terminal domain consists of an anti-parallel beta barrel overlaid by a short alpha helical region [1,5]. This domain is highly similar to Transferrin-binding protein B beta barrel (Pfam:PF01298).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	LIPOPROTEIN	-	-	membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle bacterial extracellular vesicle vesicle extracellular membrane-bounded organelle cell periphery cell outer membrane external encapsulating structure membrane cell envelope membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle bacterial extracellular vesicle vesicle extracellular membrane-bounded organelle cell periphery cell outer membrane external encapsulating structure membrane cell envelope outer membrane
B [auth H]	FAB 12C1	-	-	-
C [auth L]	FAB 12C1	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011250	Outer membrane protein/outer membrane enzyme PagP, beta-barrel	Homologous Superfamily
A	IPR014902	Factor H binding protein-like, C-terminal	Domain
A	IPR049377	Factor H binding protein, N-terminal	Domain
A	IPR049378	Factor H binding protein	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.