1DLE: Factor B serine protease domain

Factor B serine protease domain. Determined by X-ray diffraction at 2.1 Å resolution. Released 13 Dec 2000.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,022
Mol. weight: 67.4 kDa
Released: 13 Dec 2000

Explore 1DLE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DLE contains 32 α-helices and 30 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: 16 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	1F-1C	4
α-helix	23-26	4
β-strand	30-35	6	1
β-strand	40-46	7	1
β-strand	51-54	4	1
α-helix	56-58	3
β-strand	64-68	5	1
α-helix	82-84	3
β-strand	85-90	6	1
α-helix	97C-97E	3
β-strand	104-108	5	1
α-helix	120-121	2
β-strand	122	1	2
β-strand	125A	1	3
α-helix	125B-125G	6
α-helix	125P-128	8
β-strand	133-142	10	2
β-strand	154-163	10	2
α-helix	165-170	6
α-helix	171-172B	4
α-helix	172L-174	3
β-strand	180-184	5	2
α-helix	192-194	3
α-helix	197	1
β-strand	198-201	4	2
β-strand	208-216	9	2
α-helix	221-223	3
β-strand	225-230	6	2
α-helix	231-234	4
α-helix	235-241	7
β-strand	249	1	3

Chain B: 16 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	23-26	4
β-strand	30-35	6	4
β-strand	40-46	7	4
β-strand	51-54	4	4
α-helix	56-58	3
β-strand	64-68	5	4
α-helix	82-84	3
β-strand	85-90	6	4
α-helix	91	1
α-helix	97C-97E	3
β-strand	104-108	5	4
α-helix	111-112	2
β-strand	122	1	5
β-strand	125A	1	6
α-helix	125B-125G	6
α-helix	125P-128	8
β-strand	133-142	10	5
β-strand	154-163	10	5
α-helix	165-170	6
α-helix	171-172B	4
α-helix	172L-174	3
β-strand	180-184	5	5
α-helix	192-194	3
α-helix	197	1
β-strand	198-203	6	5
β-strand	206-216	11	5
α-helix	221-223	3
β-strand	225-230	6	5
α-helix	231-233	3
α-helix	235-241	7
β-strand	249	1	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement factor B	A, B	protein	298	Homo sapiens	P00751 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1DLE_1 COMPLEMENT FACTOR B (chains A, B)
ADPDESQSLSLCGMVWEHRKGTDYHKQPWQAKISVIRPSKGHESCMGAVVSEYFVLTAAH
CFTVDDKEHSIKVSVGGEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLKNKL
KYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEELLPAQDIKALFVSEEEKKLTRKEVY
IKNGDKKGSCERDAQYAPGYDKVKDISEVVTPRFLCTGGVSPYADPNTCRGDSGGPLIVH
KRSRFIQVGVISWGVVDVCKNQKRQKQVPAHARDFHINLFQVLPWLKEKLQDEDLGFL

Primary citation

New structural motifs on the chymotrypsin fold and their potential roles in complement factor B. Jing, H., Xu, Y., Carson, M. et al. EMBO J (2000) 19:164-173. DOI 10.1093/emboj/19.2.164 · PubMed

Other PDB entries of the same protein (UniProt P00751 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6QSW 1.64 Å, Complement factor B protease domain in complex with the reversible inhibitor…
6RAV 1.7 Å, Complement factor B protease domain in complex with the reversible inhibitor…
6T8W 1.7 Å, Complement factor B in complex with (-)-4-(1-((5,7-Dimethyl-1H-indol-4-yl)methyl)piperidi…
6QSX 1.77 Å, Complement factor B protease domain in complex with the reversible inhibitor…
1Q0P 1.8 Å, A domain of Factor B
1RRK 2.0 Å, Crystal Structure Analysis of the Bb segment of Factor B
3HRZ 2.2 Å, Cobra Venom Factor (CVF) in complex with human factor B
6T8V 2.29 Å, Complement factor B in complex with (S)-5,7-Dimethyl-4-((2-phenylpiperidin-1-yl)methyl)-1…
1RTK 2.3 Å, Crystal Structure Analysis of the Bb segment of Factor B complexed with…
2OK5 2.3 Å, Human Complement factor B
1RS0 2.6 Å, Crystal Structure Analysis of the Bb segment of Factor B complexed with…
9U62 2.7 Å, AP pathways C3 convertase C3bBbP and C3 complex

Browse structure collections

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