2OAY: Latent human C1-inhibitor

Crystal structure of latent human C1-inhibitor. Determined by X-ray diffraction at 2.35 Å resolution. Released 1 May 2007.

Method: X-ray diffraction
Resolution: 2.35 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,960
Mol. weight: 44.4 kDa
Ligands: NAG
Released: 1 May 2007

Explore 2OAY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2OAY contains 14 α-helices and 17 β-strands across 1 chain. 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: 14 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	113-135	23
β-strand	145-147	3	1
α-helix	149-161	13
α-helix	165-175	11
α-helix	184-189	6
β-strand	196-204	9	2
α-helix	209-211	3
α-helix	212-222	11
β-strand	227-228	2	2
α-helix	233-246	14
β-strand	265-276	12	2
β-strand	277	1	3
α-helix	280-282	3
β-strand	287-291	5	1
β-strand	298-315	18	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	367-368	2
β-strand	369-377	9	1
β-strand	380-386	7	2
α-helix	387-391	5
α-helix	392-394	3
α-helix	399-402	4
β-strand	419-427	9	2
β-strand	431-440	10	2
β-strand	446-448	3	2
β-strand	455-461	7	1
β-strand	466-473	8	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Plasma protease C1 inhibitor	A	protein	390	Homo sapiens	P05155 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2OAY_1 Plasma protease C1 inhibitor (chains A)
YVHHHHHHTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFS
PFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDL
AIRDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLL
NAIYLSAKWKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLS
HNLSLVILVPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDML
SIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLV
FEVQQPFLFMLWDQQHKFPVFMGRVYDPRA

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1

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

Primary citation

C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease. Beinrohr, L., Harmat, V., Dobo, J. et al. J Biol Chem (2007) 282:21100-21109. DOI 10.1074/jbc.M700841200 · 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
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

Browse structure collections

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