4IGD: Zymogen catalytic region of Human MASP-1

Crystal structure of the zymogen catalytic region of Human MASP-1. Determined by X-ray diffraction at 2.5 Å resolution. Released 13 Feb 2013.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,152
Mol. weight: 45.67 kDa
Released: 13 Feb 2013

Explore 4IGD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4IGD contains 19 α-helices and 43 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: 19 helices, 43 β-strands

Element	Residues	Length	Sheet
β-strand	300-301	2	1
α-helix	302-304	3
α-helix	306-307	2
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
α-helix	365	1
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
α-helix	405-407	3
β-strand	411-414	4	6
β-strand	420-422	3	6
β-strand	426	1	6
α-helix	429-430	2
β-strand	432-434	3	7
α-helix	435	1
β-strand	453-454	2	8
α-helix	455-456	2
β-strand	463-468	6	9
β-strand	473-480	8	9
β-strand	484-487	4	9
α-helix	489-491	3
β-strand	493	1	10
α-helix	494-496	3
β-strand	497	1	11
β-strand	500	1	11
β-strand	508	1	10
α-helix	509-510	2
β-strand	514-518	5	9
β-strand	522	1	12
β-strand	531-540	10	9
β-strand	545	1	13
β-strand	550	1	13
β-strand	554-558	5	9
β-strand	565	1	14
β-strand	568	1	14
α-helix	570-571	2
β-strand	572	1	8
α-helix	573-574	2
β-strand	583-588	6	8
β-strand	600	1	12
β-strand	602-609	8	8
α-helix	610	1
α-helix	611-618	8
α-helix	619-621	3
β-strand	629-632	4	8
β-strand	649-654	6	8
β-strand	659-666	8	8
α-helix	672-675	4
β-strand	679-683	5	8
α-helix	684-687	4
α-helix	688-695	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mannan-binding lectin serine protease 1	A	protein	406	Homo sapiens	P48740 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4IGD_1 Mannan-binding lectin serine protease 1 (chains A)
ASMTGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDG
TWSNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYT
CSAQGVWMNKVLGRSLPTCLPVCGLPKFSRKLMAQIFNGRPAQKGTTPWIAMLSHLNGQP
FCGGSLLGSSWIVTAAHCLHQSLDPEDPTLRDSDLLSPSDFKIILGKHWRLRSDENEQHL
GVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVSGWGKQF
LQRFPETLMEIEIPIVDHSTCQKAYAPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTL
NRERGQWYLVGTVSWGDDCGKKDRYGVYSYIHHNKDWIQRVTGVRN

Primary citation

Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway. Megyeri, M., Harmat, V., Major, B. et al. J Biol Chem (2013) 288:8922-8934. DOI 10.1074/jbc.M112.446500 · 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
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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