6F39: C1r homodimer CUB1-EGF-CUB2

C1r homodimer CUB1-EGF-CUB2. Determined by X-ray diffraction at 5.8 Å resolution. Released 24 Jan 2018.

Method: X-ray diffraction
Resolution: 5.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,612
Mol. weight: 67.59 kDa
Ligands: NAG, CA
Released: 24 Jan 2018

Explore 6F39 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6F39 contains 13 α-helices and 52 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: 6 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	10-13	4	1
α-helix	14	1
α-helix	20-22	3
β-strand	25-32	8	2
α-helix	33-34	2
β-strand	41-42	2	1
β-strand	47	1	3
β-strand	57-61	5	2
β-strand	69-71	3	2
β-strand	94-101	8	2
β-strand	116	1	3
β-strand	118-121	4	1
β-strand	147-148	2	4
β-strand	151	1	5
β-strand	154	1	5
β-strand	157-158	2	4
β-strand	179-181	3	6
β-strand	186-189	4	7
α-helix	196-198	3
β-strand	202-208	7	6
α-helix	209-210	2
β-strand	214-220	7	7
β-strand	225	1	8
β-strand	237-242	6	6
β-strand	245-250	6	6
β-strand	252	1	8
α-helix	255-258	4
β-strand	259-260	2	7
β-strand	265-271	7	6
β-strand	282-288	7	7

Chain B: 7 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	10	1	9
β-strand	13	1	10
α-helix	14	1
α-helix	20-22	3
β-strand	25-32	8	11
α-helix	33-34	2
β-strand	37	1	12
β-strand	40-42	3	9
β-strand	47	1	13
β-strand	57-62	6	11
β-strand	67-71	5	11
β-strand	94-101	8	11
α-helix	107-109	3
β-strand	116	1	13
β-strand	118	1	10
β-strand	120-122	3	9
β-strand	125	1	12
β-strand	151	1	14
β-strand	154	1	14
β-strand	186-189	4	15
α-helix	196-198	3
β-strand	202-205	4	16
β-strand	208	1	17
α-helix	209-210	2
β-strand	215-220	6	15
β-strand	225	1	18
β-strand	237	1	16
β-strand	239-242	4	16
β-strand	245-249	5	16
β-strand	252	1	18
α-helix	255-258	4
β-strand	259-260	2	15
β-strand	265	1	17
β-strand	266-271	6	16
β-strand	282-287	6	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement C1r subcomponent	A, B	protein	285	Homo sapiens	P00736 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6F39_1 Complement C1r subcomponent (chains A, B)
PQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVKISAD
KKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAV
DLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSELYTEA
SGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQIYANG
KNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEI

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1
CA	Calcium ion	Ca	6

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

Primary citation

Structure of the C1r-C1s interaction of the C1 complex of complement activation. Almitairi, J.O.M., Venkatraman Girija, U., Furze, C.M. et al. Proc Natl Acad Sci U S A (2018) 115:768-773. DOI 10.1073/pnas.1718709115 · 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
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
1APQ Structure of the egf-like module of human C1R, NMR, 19 structures

Browse structure collections

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