3GOV: Catalytic region of human MASP-1

Crystal structure of the catalytic region of human MASP-1. Determined by X-ray diffraction at 2.55 Å resolution. Released 9 Jun 2009.

Method: X-ray diffraction
Resolution: 2.55 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,196
Mol. weight: 45.72 kDa
Released: 9 Jun 2009

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

Secondary structure: helices and β-sheets

3GOV contains 15 α-helices and 43 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: 3 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	299	1
β-strand	300-301	2	1
α-helix	302-307	6
β-strand	310-313	4	2
β-strand	319-320	2	1
β-strand	324-329	6	2
β-strand	333-337	5	3
β-strand	340-342	3	3
β-strand	344-348	5	2
β-strand	349	1	4
β-strand	355	1	4
β-strand	361-364	4	3
β-strand	366	1	5
α-helix	370-372	3
β-strand	376-380	5	6
β-strand	388	1	5
β-strand	392-397	6	6
β-strand	402-404	3	7
β-strand	411-414	4	6
β-strand	420-421	2	6
β-strand	422	1	8
β-strand	426	1	8
β-strand	432-434	3	7

Chain B: 12 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	450	1	9
β-strand	453-454	2	10
α-helix	455-456	2
β-strand	463-468	6	11
β-strand	473-480	8	11
β-strand	484-487	4	11
α-helix	489-492	4
β-strand	493	1	12
α-helix	494-497	4
α-helix	505-507	3
β-strand	508	1	12
α-helix	509-510	2
α-helix	511-513	3
β-strand	514-518	5	11
β-strand	522	1	13
β-strand	531-533	3	11
β-strand	535-540	6	11
β-strand	545	1	14
β-strand	550	1	14
β-strand	554-558	5	11
α-helix	570-571	2
β-strand	572	1	10
α-helix	573-574	2
α-helix	578-579	2
β-strand	583-588	6	10
β-strand	600	1	13
β-strand	602-609	8	10
α-helix	610	1
α-helix	611-617	7
β-strand	629-632	4	10
β-strand	640	1	9
β-strand	649-653	5	10
β-strand	660-668	9	10
β-strand	679-683	5	10
α-helix	688-695	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Masp-1	A	protein	155	Homo sapiens	P48740 (AlphaFold model)
Masp-1	B	protein	251	Homo sapiens	P48740 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3GOV_1 MASP-1 (chains A)
ASMTGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDG
TWSNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYT
CSAQGVWMNKVLGRSLPTCLPVCGLPKFSRKLMAR

Sequence of entity 2 (B), FASTA

>3GOV_2 MASP-1 (chains B)
IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSLDPKDPTLRDSDL
LSPSDFKIILGKHWRLRSDENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFV
MPICLPEGPQQEGAMVIVSGWGKQFLQRFPETLMEIEIPIVDHSTCQKAYAPLKKKVTRD
MICAGEKEGGKDACAGDSGGPMVTLNRERGQWYLVGTVSWGDDCGKKDRYGVYSYIHHNK
DWIQRVTGVRN

Primary citation

MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity. Dobo, J., Harmat, V., Beinrohr, L. et al. J Immunol (2009) 183:1207-1214. DOI 10.4049/jimmunol.0901141 · PubMed

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

3DEM 2.3 Å, CUB1-EGF-CUB2 domain of HUMAN MASP-1/3
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
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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