5DUQ: Active human c1-inhibitor

Active human c1-inhibitor in complex with dextran sulfate. Determined by X-ray diffraction at 2.9 Å resolution. Released 31 Aug 2016.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,840
Mol. weight: 86.87 kDa
Ligands: NAG, SO3, GLC
Released: 31 Aug 2016

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

Secondary structure: helices and β-sheets

5DUQ contains 30 α-helices and 46 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: 15 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	116-138	23
β-strand	145-147	3	1
α-helix	149-161	13
α-helix	165-174	10
α-helix	184-191	8
β-strand	196-199	4	2
β-strand	202-204	3	3
β-strand	210	1	4
α-helix	212-221	10
α-helix	233-246	14
β-strand	265-267	3	3
β-strand	270-273	4	2
β-strand	277-279	3	5
α-helix	280-282	3
α-helix	283-285	3
β-strand	288-291	4	6
β-strand	298-301	4	6
β-strand	302-310	9	7
β-strand	311-315	5	1
β-strand	320-326	7	1
β-strand	327	1	5
β-strand	331-338	8	1
α-helix	345-349	5
α-helix	354-366	13
α-helix	368-369	2
β-strand	370-377	8	7
α-helix	378	1
β-strand	379-386	8	2
α-helix	387-393	7
β-strand	409	1	4
β-strand	418-419	2	3
β-strand	420-427	8	2
β-strand	431-433	3	5
α-helix	434-435	2
α-helix	436-439	4
β-strand	448-450	3	7
β-strand	455-461	7	1
β-strand	466-473	8	1

Chain B: 15 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	115-138	24
β-strand	145-147	3	8
α-helix	149-161	13
α-helix	165-174	10
α-helix	184-191	8
β-strand	196-199	4	9
β-strand	202-204	3	10
β-strand	210	1	11
α-helix	212-221	10
α-helix	233-247	15
β-strand	265-267	3	10
β-strand	270-273	4	9
β-strand	277-279	3	12
α-helix	280-282	3
α-helix	283-285	3
β-strand	288-291	4	13
β-strand	298-301	4	13
β-strand	302-310	9	14
β-strand	311-315	5	8
β-strand	320-326	7	8
β-strand	327	1	12
β-strand	331-338	8	8
α-helix	345-349	5
α-helix	354-366	13
α-helix	368-369	2
β-strand	370-377	8	14
α-helix	378	1
β-strand	379-386	8	9
α-helix	387-393	7
β-strand	409	1	11
β-strand	418-419	2	10
β-strand	420-427	8	9
β-strand	431-433	3	12
α-helix	434-435	2
α-helix	436-439	4
β-strand	448-450	3	14
β-strand	455-461	7	8
β-strand	466-473	8	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Plasma protease C1 inhibitor	A, B	protein	383	Homo sapiens	P05155 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5DUQ_1 Plasma protease C1 inhibitor (chains A, B)
TTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASL
LTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFV
NASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSA
KWKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVI
LVPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLE
FFDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLVFEVQQPF
LFMLWDQQHKFPVFMGRVYDPRA

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	2
SO3	Sulfite ion	O3 S	1
GLC	alpha-D-glucopyranose	C6 H12 O6	1

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:

5DU3 2.1 Å, Active form of human C1-inhibitor
2OAY 2.35 Å, Crystal structure of latent human C1-inhibitor
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

Browse structure collections

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