5DU3: Active form of human C1-inhibitor

Active form of human C1-inhibitor. Determined by X-ray diffraction at 2.1 Å resolution. Released 31 Aug 2016.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,097
Mol. weight: 85.56 kDa
Released: 31 Aug 2016

Explore 5DU3 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5DU3 contains 36 α-helices and 35 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: 18 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	102-109	8
α-helix	110-115	6
α-helix	117-138	22
β-strand	145-147	3	1
α-helix	149-160	12
α-helix	165-175	11
α-helix	177-178	2
α-helix	184-190	7
β-strand	196-204	9	2
α-helix	209-211	3
α-helix	212-222	11
β-strand	227-228	2	2
α-helix	229-230	2
α-helix	233-247	15
β-strand	265-273	9	2
β-strand	277-279	3	3
α-helix	280-281	2
α-helix	283-285	3
β-strand	287-293	7	1
β-strand	296-315	20	1
β-strand	320-326	7	1
β-strand	327	1	3
β-strand	331-338	8	1
α-helix	345-351	7
α-helix	354-365	12
α-helix	368-369	2
β-strand	370-377	8	1
β-strand	379-386	8	2
α-helix	387-393	7
β-strand	418-427	10	2
β-strand	431-433	3	3
α-helix	434-436	3
β-strand	447-450	4	1
β-strand	455-461	7	1
β-strand	466-473	8	1

Chain B: 18 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	104-109	6
α-helix	110-114	5
α-helix	117-138	22
α-helix	140	1
β-strand	145-147	3	4
α-helix	149-160	12
α-helix	165-175	11
α-helix	177-178	2
α-helix	184-190	7
β-strand	196-204	9	5
α-helix	209-211	3
α-helix	212-221	10
β-strand	227-228	2	5
α-helix	233-247	15
β-strand	265-273	9	5
β-strand	277-279	3	6
α-helix	280-281	2
α-helix	283-285	3
β-strand	287-293	7	7
β-strand	296-310	15	7
β-strand	311-315	5	4
β-strand	320-326	7	4
β-strand	327	1	6
β-strand	331-338	8	4
α-helix	345-351	7
α-helix	354-366	13
α-helix	368-369	2
β-strand	370-377	8	7
β-strand	379-386	8	5
α-helix	387-393	7
β-strand	418-427	10	5
β-strand	431-433	3	6
α-helix	434-436	3
β-strand	447-450	4	7
β-strand	455-461	7	4
β-strand	466-473	8	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Plasma protease C1 inhibitor	A, B	protein	382	Homo sapiens	P05155 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5DU3_1 Plasma protease C1 inhibitor (chains A, B)
TGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASLL
TQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFVN
ASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAK
WKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVIL
VPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEF
FDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLVFEVQQPFL
FVLWDQQHKFPVFMGRVYDPRA

Primary citation

How Dextran Sulfate Affects C1-inhibitor Activity: A Model for Polysaccharide Potentiation. Dijk, M., Holkers, J., Voskamp, P. et al. Structure (2016) 24:2182-2189. DOI 10.1016/j.str.2016.09.013 · PubMed

Other PDB entries of the same protein (UniProt P05155 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2OAY 2.35 Å, Crystal structure of latent human C1-inhibitor
5DUQ 2.9 Å, Active human c1-inhibitor in complex with dextran sulfate
7AKV 3.6 Å, The cryo-EM structure of the Vag8-C1 inhibitor complex
8W18 3.94 Å, The crystal structure of the Michaelis-Menten complex of a C1s/C1-INH at 3.94 Angstroms

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