8EO2: Lufaxin

Lufaxin a bifunctional inhibitor of complement and coagulation. Determined by X-ray diffraction at 2.31 Å resolution. Released 9 Aug 2023.

Method: X-ray diffraction
Resolution: 2.31 Å
Organism: Lutzomyia longipalpis
Chains: 2
Atoms: 4,686
Mol. weight: 68.65 kDa
Ligands: NAG
Released: 9 Aug 2023

Explore 8EO2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8EO2 contains 16 α-helices and 48 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: 8 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	1
α-helix	14	1
β-strand	15-23	9	1
β-strand	32	1	2
β-strand	35	1	2
β-strand	37-39	3	3
β-strand	43-49	7	3
β-strand	54-64	11	1
α-helix	71-73	3
β-strand	77-82	6	3
β-strand	88-94	7	3
β-strand	101-110	10	1
α-helix	117-121	5
β-strand	128	1	4
α-helix	133	1
β-strand	134	1	4
α-helix	135	1
β-strand	137	1	5
β-strand	143	1	6
β-strand	144	1	5
α-helix	145-147	3
β-strand	151-154	4	7
β-strand	160-164	5	7
β-strand	167-172	6	7
β-strand	176	1	6
β-strand	180-188	9	7
α-helix	189-191	3
β-strand	195-201	7	8
α-helix	204-206	3
β-strand	208-217	10	7
β-strand	228-231	4	8
β-strand	241-247	7	8
β-strand	252-261	10	7

Chain B: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-8	6	9
α-helix	14	1
β-strand	15-23	9	9
β-strand	37-39	3	10
β-strand	43-49	7	10
β-strand	54-64	11	9
β-strand	77-82	6	10
β-strand	88-94	7	10
β-strand	101-110	10	9
α-helix	111-113	3
α-helix	117-121	5
β-strand	128	1	11
α-helix	133	1
β-strand	134	1	11
α-helix	135	1
β-strand	137	1	12
β-strand	143	1	13
β-strand	144	1	12
α-helix	145-147	3
β-strand	151-154	4	14
β-strand	160-164	5	14
β-strand	167-172	6	14
β-strand	176	1	13
β-strand	180-188	9	14
α-helix	189-191	3
β-strand	195-201	7	15
α-helix	204-206	3
β-strand	208-217	10	14
β-strand	228-231	4	15
β-strand	241-247	7	15
β-strand	252-261	10	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lufaxin	A, B	protein	284	Lutzomyia longipalpis	Q5WPU8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8EO2_1 Lufaxin (chains A, B)
DGDEYFIGKYKEKDETLFFASYGLKRDPCQIVLGYKCSNNQTHFVLNFKTNKKSCISAIK
LTSYPKINQNSDLTRNLYCQTGGIGTDNCKLVFKKRKRQIAANIEIYGIPAKKCSFKDRY
IGADPLHVDSYGLSYQFDQEHGWNLERNNIFKDTRFSTEVFYHKNGLFNTQITYLAEEDS
FSEAREITAKDIKKKFSIILPNEEYKRISFLDVYWFQETMRKKPKYPYIHYNGECSNENK
TCELVFDTDELMTYALVKVFTNPESDGSRLKEEDLGRGHHHHHH

Ligands and cofactors

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

Water and common crystallization additives (GOL, BR) are not listed.

Primary citation

A bispecific inhibitor of complement and coagulation blocks activation in complementopathy models via a novel mechanism. Andersen, J.F., Lei, H., Strayer, E.C. et al. Blood (2023) 141:3109-3121. DOI 10.1182/blood.2022019359 · PubMed

Other PDB entries of the same protein (UniProt Q5WPU8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8ENU 3.22 Å, Structure of the C3bB proconvertase in complex with lufaxin
8EOK 3.53 Å, Structure of the C3bB proconvertase in complex with lufaxin and factor Xa

Browse structure collections

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