4CBN: Complement factor D

Crystal structure of Complement Factor D mutant R202A after conventional refinement. Determined by X-ray diffraction at 1.8 Å resolution. Released 18 Dec 2013.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 3,936
Mol. weight: 48.98 kDa
Released: 18 Dec 2013

Explore 4CBN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4CBN contains 16 α-helices and 42 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, 20 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	1
β-strand	5-6	2	2
α-helix	7-8	2
β-strand	15-20	6	3
β-strand	23-32	10	3
β-strand	35-38	4	3
α-helix	40-42	3
β-strand	51-55	5	3
β-strand	59	1	4
β-strand	68-77	10	3
β-strand	91-95	5	3
β-strand	102	1	5
β-strand	105	1	5
β-strand	110	1	2
α-helix	116-118	3
β-strand	122-127	6	2
α-helix	136-138	3
β-strand	140	1	4
β-strand	142-149	8	2
α-helix	150	1
α-helix	151-154	4
β-strand	168-171	4	2
β-strand	177	1	1
β-strand	186-189	4	2
β-strand	192-197	6	2
β-strand	211-215	5	2
α-helix	216-219	4
α-helix	220-227	8

Chain B: 8 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	6
β-strand	5-6	2	7
α-helix	7-8	2
β-strand	15-20	6	8
β-strand	23-32	10	8
β-strand	35-38	4	8
α-helix	40-44	5
β-strand	51-55	5	8
β-strand	59	1	9
β-strand	68-77	10	8
β-strand	91-95	5	8
α-helix	98-101	4
β-strand	102	1	10
β-strand	105	1	10
β-strand	110	1	7
α-helix	116-118	3
β-strand	122-127	6	7
α-helix	136-138	3
β-strand	140	1	9
β-strand	142-149	8	7
α-helix	151-154	4
β-strand	168-171	4	7
β-strand	177	1	6
β-strand	179	1	11
β-strand	186-189	4	7
β-strand	192-197	6	7
β-strand	201	1	11
β-strand	211-215	5	7
α-helix	216-219	4
α-helix	220-227	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement factor D	A, B	protein	228	HOMO SAPIENS	P00746 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4CBN_1 COMPLEMENT FACTOR D (chains A, B)
ILGGREAEAHARPYMASVQLNGAHLCGGVLVAEQWVLSAAHCLEDAADGKVQVLLGAHSL
SQPEPSKRLYDVLRAVPHPDSQPDTIDHDLLLLQLSEKATLGPAVRPLPWQRVDRDVAPG
TLCDVAGWGIVNHAGRRPDSLQHVLLPVLDRATCNRRTHHDGAITERLMCAESNRRDSCK
GDSGGPLVCGGVLEGVVTSGSAVCGNRKKPGIYTRVASYAAWIDSVLA

Primary citation

Ensemble Refinement Shows Conformational Flexibility in Crystal Structures of Human Complement Factor D. Forneris, F., Burnley, B.T., Gros, P. Acta Crystallogr D Biol Crystallogr (2014) 70:733. DOI 10.1107/S1399004713032549 · PubMed

Other PDB entries of the same protein (UniProt P00746 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5NAT 1.17 Å, Complement factor D in complex with the inhibitor (S)-Pyrrolidine-1,2-dicarboxylic acid…
2XW9 1.2 Å, Crystal Structure of Complement Factor D mutant S183A
5NAW 1.25 Å, Complement factor D in complex with the inhibitor (1R,3S,5R)-2-Aza-bicyclo[3.1.0]hexane-2…
5MT0 1.29 Å, Complement factor D in complex with a reversible indole carboxylic acid based inhibitor
5NB7 1.33 Å, Complement factor D
6FUH 1.37 Å, Complement factor D in complex with the inhibitor (4-((3-(aminomethyl)phenyl)amino)quinaz…
6FUI 1.38 Å, Complement factor D in complex with the inhibitor 3-((3-((3-(aminomethyl)phenyl)amino)-1H…
5FBE 1.43 Å, Complement factor D in complex with COMPOUND2
5FBI 1.47 Å, Complement factor D in complex with compound 3b
1BIO 1.5 Å, Human complement factor D in complex with isatoic anhydride inhibitor
6FUT 1.5 Å, Complement factor D in complex with the inhibitor (S)-3'-(aminomethyl)-N-(1,2,3,4-tetrahy…
5NAR 1.55 Å, Complement factor D in complex with the inhibitor (S)-pyrrolidine-1,2-dicarboxylic acid…

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