1MD7: C1R complement serine protease

Monomeric structure of the zymogen of complement protease C1r. Determined by X-ray diffraction at 3.2 Å resolution. Released 7 Aug 2003.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,531
Mol. weight: 37.28 kDa
Ligands: NAG
Released: 7 Aug 2003

Explore 1MD7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1MD7 contains 9 α-helices and 22 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: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	368-372	5	1
β-strand	384-389	6	1
α-helix	390	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
β-strand	452	1	3
β-strand	461-466	6	4
β-strand	468-475	8	4
β-strand	479-482	4	4
α-helix	484-487	4
α-helix	489-490	2
β-strand	502-504	3	4
β-strand	508	1	5
α-helix	509-515	7
β-strand	520-525	6	4
β-strand	542-546	5	4
β-strand	560	1	3
α-helix	565-567	3
β-strand	573-578	6	3
β-strand	589	1	5
β-strand	591-597	7	3
β-strand	620-624	5	3
α-helix	629-633	5
β-strand	641-643	3	3
β-strand	652-657	6	3
β-strand	667-672	6	3
α-helix	673-676	4
α-helix	677-684	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
C1R complement serine protease	A	protein	328	Homo sapiens	P00736 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1MD7_1 C1R COMPLEMENT SERINE PROTEASE (chains A)
DCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGI
WKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGD
RWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDESYNF
EGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHDLRFVRLPV
ANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDAGGVFAVRDPNTDRWVATGIV
SWGIGCSRGYGFYTKVLNYVDWIKKEME

Ligands and cofactors

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

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…
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
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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