1MD8: C1R complement serine protease

Monomeric structure of the active catalytic domain of complement protease C1r. Determined by X-ray diffraction at 2.8 Å resolution. Released 7 Aug 2003.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,576
Mol. weight: 37.2 kDa
Released: 7 Aug 2003

Explore 1MD8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MD8 contains 11 α-helices and 28 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: 11 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	362-364	3
β-strand	368-372	5	1
β-strand	384-389	6	1
β-strand	394-396	3	2
β-strand	409-412	4	1
β-strand	418-419	2	1
β-strand	430-432	3	2
α-helix	433-434	2
α-helix	440-442	3
β-strand	448	1	3
β-strand	452	1	4
α-helix	453-454	2
β-strand	461-465	5	5
β-strand	469-475	7	5
β-strand	479-482	4	5
α-helix	484-486	3
β-strand	502-504	3	5
β-strand	508	1	6
α-helix	509-515	7
β-strand	520-525	6	5
β-strand	542-546	5	5
β-strand	553	1	7
β-strand	556	1	7
β-strand	560	1	4
α-helix	565-568	4
β-strand	573-578	6	4
β-strand	581	1	8
β-strand	586	1	8
β-strand	589	1	6
β-strand	591-597	7	4
α-helix	598-599	2
α-helix	600-609	10
β-strand	620-623	4	4
β-strand	631	1	3
β-strand	640-645	6	4
β-strand	650-659	10	4
β-strand	668-672	5	4
α-helix	673-675	3
α-helix	677-685	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
C1R complement serine protease	A	protein	329	Homo sapiens	P00736 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1MD8_1 C1R COMPLEMENT SERINE PROTEASE (chains A)
DCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGI
WKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGD
RWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDESYNF
EGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHDLRFVRLPV
ANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTDRWVATGIV
SWGIGCSRGYGFYTKVLNYVDWIKKEMEE

Primary citation

Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism. Budayova-Spano, M., Grabarse, W., Thielens, N.M. et al. Structure (2002) 10:1509-1519. DOI 10.1016/S0969-2126(02)00881-X · 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
2QY0 2.6 Å, Active dimeric structure of the catalytic domain of C1r reveals enzyme-product like…
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

Browse structure collections

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