4DJZ: Catalytic fragment of masp-1

Catalytic fragment of masp-1 in complex with its specific inhibitor developed by directed evolution on sgci scaffold. Determined by X-ray diffraction at 3.2 Å resolution. Released 25 Apr 2012.

Method: X-ray diffraction
Resolution: 3.2 Å
Organisms: Homo sapiens, Schistocerca gregaria
Chains: 6
Atoms: 6,465
Mol. weight: 99.25 kDa
Released: 25 Apr 2012

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

Secondary structure: helices and β-sheets

4DJZ contains 36 α-helices and 93 β-strands across 6 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, 20 β-strands

Element	Residues	Length	Sheet
β-strand	300-301	2	1
α-helix	302-304	3
α-helix	306-307	2
β-strand	312-313	2	2
β-strand	319-320	2	1
β-strand	324-328	5	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	411-415	5	6
β-strand	419-421	3	6
β-strand	422	1	8
β-strand	426	1	8
α-helix	429-430	2
β-strand	432-434	3	7

Chain B: 14 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	450	1	9
β-strand	453-454	2	10
α-helix	455-456	2
β-strand	463-467	5	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	505-507	3
β-strand	508	1	12
α-helix	509-510	2
α-helix	511-513	3
β-strand	515-518	4	11
β-strand	531-533	3	11
β-strand	535-540	6	11
β-strand	554-558	5	11
α-helix	561-564	4
β-strand	565	1	13
β-strand	568	1	13
α-helix	570-571	2
β-strand	572	1	10
α-helix	573-574	2
β-strand	583-588	6	10
α-helix	593-595	3
β-strand	602-609	8	10
α-helix	610	1
α-helix	611-618	8
β-strand	629-632	4	10
β-strand	640	1	9
β-strand	649-654	6	10
β-strand	659-669	11	10
α-helix	678	1
β-strand	679-683	5	10
α-helix	685-687	3
α-helix	688-695	8

Chain C: 6 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	306-307	2
β-strand	310	1	14
β-strand	313	1	15
β-strand	324-328	5	15
β-strand	329	1	14
β-strand	333-334	2	16
β-strand	335-336	2	17
β-strand	341-342	2	17
β-strand	344-348	5	15
β-strand	349	1	18
β-strand	355	1	18
α-helix	358-361	4
β-strand	363-364	2	16
α-helix	365	1
β-strand	366	1	19
α-helix	370-373	4
β-strand	376-377	2	20
β-strand	380	1	21
β-strand	388	1	19
β-strand	392-394	3	21
β-strand	396-397	2	20
β-strand	402-404	3	22
α-helix	405-407	3
β-strand	411-414	4	21
β-strand	420-421	2	21
β-strand	422	1	23
β-strand	426	1	23
β-strand	432-434	3	22
α-helix	435-436	2

Chain D: 10 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	450	1	24
β-strand	453-454	2	25
α-helix	455-456	2
β-strand	463-468	6	26
β-strand	473-480	8	26
β-strand	484-488	5	26
α-helix	489-492	4
β-strand	493	1	27
β-strand	508	1	27
α-helix	509-510	2
β-strand	514-518	5	26
β-strand	522	1	28
β-strand	531-533	3	26
β-strand	535-540	6	26
β-strand	553-558	6	26
β-strand	565	1	29
β-strand	568	1	29
α-helix	570-571	2
β-strand	572	1	25
α-helix	573-574	2
α-helix	577-579	3
β-strand	583-588	6	25
α-helix	593-595	3
β-strand	600	1	28
β-strand	602-609	8	25
α-helix	610	1
α-helix	611-618	8
β-strand	629-632	4	25
β-strand	640	1	24
β-strand	649-653	5	25
β-strand	660-669	10	25
β-strand	679-683	5	25
α-helix	684-694	11

Chains H and I: 0 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	12-15	4	10
β-strand	18-22	5	10
β-strand	29-32	4	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mannan-binding lectin serine protease 1 heavy chain	A, C	protein	155	Homo sapiens	P48740 (AlphaFold model)
Mannan-binding lectin serine protease 1 light chain	B, D	protein	251	Homo sapiens	P48740 (AlphaFold model)
Protease inhibitor SGPI-2	H, I	protein	38	Schistocerca gregaria	O46162 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>4DJZ_1 Mannan-binding lectin serine protease 1 heavy chain (chains A, C)
ASMTGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDG
TWSNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYT
CSAQGVWMNKVLGRSLPTCLPVCGLPKFSRKLMAR

Sequence of entity 2 (B, D), FASTA

>4DJZ_2 Mannan-binding lectin serine protease 1 light chain (chains B, D)
IFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSLDPKDPTLRDSDL
LSPSDFKIILGKHWRLRSDENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFV
MPICLPEGPQQEGAMVIVSGWGKQFLQRFPETLMEIEIPIVDHSTCQKAYAPLKKKVTRD
MICAGEKEGGKDACAGDSGGPMVTLNRERGQWYLVGTVSWGDDCGKKDRYGVYSYIHHNK
DWIQRVTGVRN

Sequence of entity 3 (H, I), FASTA

>4DJZ_3 Protease inhibitor SGPI-2 (chains H, I)
GSGEVTCEPGTTFKDKCNTCRCGSDGKSAFCTRKLCYQ

Primary citation

Monospecific Inhibitors Show That Both Mannan-binding Lectin-associated Serine Protease-1 (MASP-1) and -2 Are Essential for Lectin Pathway Activation and Reveal Structural Plasticity of MASP-2. Heja, D., Harmat, V., Fodor, K. et al. J Biol Chem (2012) 287:20290-20300. DOI 10.1074/jbc.M112.354332 · 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
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…
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

Browse structure collections

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