2QY0: Complement C1r subcomponent

Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like contacts. Determined by X-ray diffraction at 2.6 Å resolution. Released 5 Feb 2008.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,306
Mol. weight: 91.85 kDa
Released: 5 Feb 2008

Explore 2QY0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2QY0 contains 26 α-helices and 81 β-strands across 4 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: 2 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	291	1	1
α-helix	293-295	3
β-strand	302-305	4	2
β-strand	312	1	1
β-strand	316-321	6	2
β-strand	325-329	5	3
β-strand	332-334	3	3
β-strand	338-340	3	2
β-strand	341	1	4
β-strand	347	1	4
β-strand	353-356	4	3
β-strand	358	1	5
α-helix	362-364	3
β-strand	368-372	5	6
β-strand	380	1	5
β-strand	384-389	6	6
β-strand	394-396	3	7
β-strand	409-412	4	6
β-strand	418-419	2	6
β-strand	420	1	8
β-strand	424	1	8
β-strand	430-432	3	7

Chain B: 11 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	448	1	9
β-strand	451-452	2	10
α-helix	453-454	2
β-strand	461-465	5	11
β-strand	469-475	7	11
β-strand	479-482	4	11
α-helix	484-487	4
β-strand	501-504	4	11
β-strand	508	1	12
α-helix	509-515	7
β-strand	520-525	6	11
β-strand	542-546	5	11
α-helix	549-552	4
β-strand	553	1	13
β-strand	556	1	13
α-helix	558-559	2
β-strand	560	1	10
α-helix	561-562	2
α-helix	565-568	4
β-strand	573-578	6	10
β-strand	589	1	12
β-strand	591-597	7	10
α-helix	600-609	10
β-strand	620-623	4	10
β-strand	631	1	9
α-helix	639	1
β-strand	640-644	5	10
β-strand	651-659	9	10
β-strand	668-672	5	10
α-helix	673-676	4
α-helix	677-683	7

Chain C: 3 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	291-292	2	14
α-helix	293-295	3
β-strand	302-304	3	15
β-strand	311-312	2	14
β-strand	316-318	3	16
β-strand	319-321	3	15
β-strand	325-329	5	17
β-strand	332-334	3	17
β-strand	338-340	3	16
β-strand	341	1	18
β-strand	347	1	18
β-strand	353-356	4	17
β-strand	358	1	19
α-helix	362-364	3
β-strand	368-372	5	20
β-strand	380	1	19
β-strand	384-389	6	20
β-strand	394-396	3	21
β-strand	409-412	4	20
β-strand	418-419	2	20
β-strand	420	1	22
β-strand	424	1	22
α-helix	427-428	2
β-strand	430-432	3	21

Chain D: 10 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	448	1	23
β-strand	451-452	2	24
α-helix	453-454	2
β-strand	461-465	5	25
β-strand	469-475	7	25
β-strand	479-482	4	25
α-helix	484-486	3
β-strand	502-504	3	25
β-strand	508	1	26
α-helix	509-515	7
β-strand	520-525	6	25
β-strand	542-546	5	25
α-helix	549-552	4
β-strand	553	1	27
β-strand	556	1	27
β-strand	560	1	24
α-helix	561-562	2
α-helix	565-568	4
β-strand	573-578	6	24
β-strand	589	1	26
β-strand	591-597	7	24
α-helix	600-609	10
β-strand	620-623	4	24
β-strand	631	1	23
α-helix	639	1
β-strand	640-644	5	24
β-strand	651-659	9	24
β-strand	668-672	5	24
α-helix	673-676	4
α-helix	677-684	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement C1r subcomponent	A, C	protein	159	Homo sapiens	P00736 (AlphaFold model)
Complement C1r subcomponent	B, D	protein	242	Homo sapiens	P00736 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>2QY0_1 Complement C1r subcomponent (chains A, C)
STQACPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTW
HRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQ
GVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQR

Sequence of entity 2 (B, D), FASTA

>2QY0_2 Complement C1r subcomponent (chains B, D)
IIGGQKAKMGNFPWQVFTNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGH
TNVEELMKLGNHPIRRVSVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDT
FYDLGLMGYVSGFGVMEEKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHP
SLKQDACQGDSGGVFAVRDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEE
ED

Primary citation

Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: Structure of the active catalytic region of C1r. Kardos, J., Harmat, V., Pallo, A. et al. Mol Immunol (2008) 45:1752-1760. DOI 10.1016/j.molimm.2007.09.031 · PubMed

Other PDB entries of the same protein (UniProt P00736 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6F1D 1.95 Å, CUB2 domain of C1r
1MD8 2.8 Å, Monomeric structure of the active catalytic domain of complement protease C1r
1GPZ 2.9 Å, The crystal structure of the zymogen catalytic domain of complement protease C1R
9EKE 3.1 Å, Structure of a C1r Zymogen Fragment Bound to SALO, Y51F Mutant
1MD7 3.2 Å, Monomeric structure of the zymogen of complement protease C1r
9EKD 3.28 Å, Structure of a C1r Zymogen Fragment Bound to SALO
7MZT 4.07 Å, Borrelia burgdorferi BBK32-C in complex with an autolytic fragment of human C1r at 4.1A
6F1C 4.2 Å, C1rC1s complex
6F1H 4.5 Å, C1rC1s complex
6F39 5.8 Å, C1r homodimer CUB1-EGF-CUB2
1APQ Structure of the egf-like module of human C1R, NMR, 19 structures

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