1GPZ: Complement C1R component

The crystal structure of the zymogen catalytic domain of complement protease C1R. Determined by X-ray diffraction at 2.9 Å resolution. Released 31 Jul 2002.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 5,970
Mol. weight: 92.35 kDa
Ligands: NAG
Released: 31 Jul 2002

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

Secondary structure: helices and β-sheets

1GPZ contains 29 α-helices and 70 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: 14 helices, 36 β-strands

Element	Residues	Length	Sheet
β-strand	292	1	1
β-strand	302-305	4	2
β-strand	311	1	1
β-strand	316-321	6	2
β-strand	325-328	4	3
β-strand	333-334	2	3
β-strand	337-340	4	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	394-397	4	7
β-strand	409-412	4	6
β-strand	418-420	3	6
β-strand	429-432	4	7
α-helix	433-434	2
α-helix	440-442	3
β-strand	451-452	2	8
α-helix	453-454	2
β-strand	461-465	5	9
β-strand	469-475	7	9
β-strand	479-482	4	9
α-helix	484-486	3
β-strand	501-504	4	9
β-strand	508	1	10
α-helix	509-514	6
β-strand	520-525	6	9
β-strand	542-546	5	9
α-helix	549-552	4
β-strand	553	1	11
β-strand	556	1	11
β-strand	560	1	8
α-helix	561-562	2
α-helix	565-568	4
β-strand	573-578	6	8
β-strand	589	1	10
β-strand	591-598	8	8
α-helix	599	1
α-helix	600-604	5
β-strand	620-624	5	8
α-helix	626-633	8
β-strand	640-645	6	8
β-strand	650-657	8	8
β-strand	667-672	6	8
α-helix	673-676	4
α-helix	677-683	7

Chain B: 15 helices, 34 β-strands

Element	Residues	Length	Sheet
β-strand	291-292	2	12
β-strand	302-304	3	13
β-strand	311-312	2	12
β-strand	316-321	6	13
β-strand	325-329	5	14
β-strand	332-334	3	14
β-strand	337-340	4	13
β-strand	341	1	15
β-strand	347	1	15
β-strand	353-356	4	14
α-helix	357	1
β-strand	358	1	16
α-helix	362-364	3
β-strand	368-372	5	17
β-strand	380	1	16
β-strand	384-389	6	17
β-strand	394-396	3	18
β-strand	409-412	4	17
β-strand	418-419	2	17
β-strand	430-432	3	18
α-helix	433	1
α-helix	440-443	4
β-strand	448-452	5	19
α-helix	453-454	2
β-strand	461-465	5	20
β-strand	469-475	7	20
β-strand	479-482	4	20
α-helix	484-486	3
β-strand	501-504	4	20
α-helix	509-514	6
β-strand	520-525	6	20
β-strand	542-546	5	20
α-helix	549-552	4
β-strand	553	1	21
β-strand	556	1	21
β-strand	560	1	19
α-helix	561-562	2
β-strand	573-578	6	19
β-strand	591-598	8	19
α-helix	599	1
α-helix	600-602	3
β-strand	620-624	5	19
α-helix	626-628	3
α-helix	631-634	4
β-strand	640-644	5	19
β-strand	651-657	7	19
β-strand	667-672	6	19
α-helix	673-676	4
α-helix	677-683	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement C1R component	A, B	protein	399	HOMO SAPIENS	P00736 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1GPZ_1 COMPLEMENT C1R COMPONENT (chains A, B)
IKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTWHR
AMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGV
YTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQQIIGGQKAKMGNFPWQVFTNIHGR
GGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDY
RQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHD
LRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTD
RWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED

Ligands and cofactors

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

Primary citation

The Crystal Structure of the Zymogen Catalytic Domain of Complement Protease C1R Reveals that a Disruptive Mechanical Stress is Required to Trigger Activation of the C1 Complex. Budayova-Spano, M., Lacroix, M., Thielens, N. et al. EMBO J (2002) 21:231. DOI 10.1093/EMBOJ/21.3.231 · 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
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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