3DEM: CUB1-EGF-CUB2 domain of HUMAN MASP-1/3

CUB1-EGF-CUB2 domain of HUMAN MASP-1/3. Determined by X-ray diffraction at 2.3 Å resolution. Released 1 Jul 2008.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,650
Mol. weight: 64.47 kDa
Ligands: CA, NAG
Released: 1 Jul 2008

Explore 3DEM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3DEM contains 10 α-helices and 50 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: 5 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	9-13	5	1
α-helix	20-22	3
β-strand	25-32	8	2
β-strand	37-47	11	1
α-helix	52-54	3
β-strand	58-62	5	2
β-strand	67-71	5	2
β-strand	74	1	1
α-helix	86-87	2
β-strand	88-89	2	1
β-strand	94-101	8	2
β-strand	111-120	10	1
β-strand	137-141	5	3
β-strand	144-148	5	3
β-strand	154-155	2	4
β-strand	162-163	2	4
β-strand	171	1	5
β-strand	175-179	5	6
α-helix	186-188	3
β-strand	192-198	7	5
β-strand	205-209	5	6
β-strand	214	1	7
β-strand	215	1	8
β-strand	227-232	6	5
β-strand	235-240	6	5
β-strand	242	1	8
α-helix	245-248	4
β-strand	249-250	2	6
β-strand	255-261	7	5
β-strand	270	1	7
β-strand	272-277	6	6

Chain B: 5 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	9-13	5	9
α-helix	20-22	3
β-strand	25-32	8	10
β-strand	37-47	11	9
α-helix	52-54	3
β-strand	58-62	5	10
β-strand	67-71	5	10
β-strand	74	1	9
α-helix	86-87	2
β-strand	88-89	2	9
β-strand	94-101	8	10
β-strand	111-120	10	9
β-strand	137-141	5	11
β-strand	144-148	5	11
β-strand	154-155	2	12
β-strand	162-163	2	12
β-strand	171	1	13
β-strand	175-179	5	14
α-helix	186-188	3
β-strand	192-198	7	13
β-strand	205-214	10	14
β-strand	215	1	15
β-strand	227-232	6	13
β-strand	235-240	6	13
β-strand	242	1	15
α-helix	245-248	4
β-strand	249-250	2	14
β-strand	255-261	7	13
β-strand	270-277	8	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Complement factor MASP-3	A, B	protein	278	Homo sapiens	P48740 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3DEM_1 Complement factor MASP-3 (chains A, B)
HTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVK
VETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVD
VDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSDNLFTQRTGVITS
PDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPF
CGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAA

Ligands and cofactors

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

Primary citation

Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins. Teillet, F., Gaboriaud, C., Lacroix, M. et al. J Biol Chem (2008) 283:25715-25724. DOI 10.1074/jbc.M803551200 · PubMed

Other PDB entries of the same protein (UniProt P48740 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7ARX 2.42 Å, Crystal structure of the catalytic fragment of masp-1 in complex with SFMI1
4IGD 2.5 Å, Crystal structure of the zymogen catalytic region of Human MASP-1
3GOV 2.55 Å, Crystal structure of the catalytic region of human MASP-1
4KKD 2.6 Å, The X-ray crystal structure of Mannose-binding lectin-associated serine proteinase-3…
4DJZ 3.2 Å, Catalytic fragment of masp-1 in complex with its specific inhibitor developed by…
4IW4 3.2 Å, Crystal structure of the serine protease domain of MASP-3 in complex with ecotin
7PQO 3.39 Å, Catalytic fragment of MASP-1 in complex with P1 site mutant ecotin
4AQB 4.2 Å, MBL-Ficolin Associated Protein-1, MAP-1 aka MAP44

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