7PQO: Catalytic fragment of MASP-1

Catalytic fragment of MASP-1 in complex with P1 site mutant ecotin. Determined by X-ray diffraction at 3.39 Å resolution. Released 18 May 2022.

Method: X-ray diffraction
Resolution: 3.39 Å
Organisms: Homo sapiens, Escherichia coli (strain K12)
Chains: 6
Atoms: 11,373
Mol. weight: 191.94 kDa
Released: 18 May 2022

Explore 7PQO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7PQO contains 75 α-helices and 158 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: 21 helices, 39 β-strands

Element	Residues	Length	Sheet
β-strand	300-301	2	16
α-helix	305-307	3
β-strand	310-313	4	17
β-strand	319-320	2	16
β-strand	324-329	6	17
β-strand	333-337	5	18
β-strand	340-342	3	18
β-strand	344-348	5	17
β-strand	349	1	19
β-strand	355	1	19
β-strand	361-364	4	18
α-helix	365	1
α-helix	370-372	3
β-strand	376-380	5	20
β-strand	392-397	6	20
α-helix	398	1
β-strand	402-404	3	21
α-helix	405-407	3
β-strand	411-414	4	20
β-strand	420-421	2	20
β-strand	422	1	22
β-strand	426	1	22
β-strand	432-434	3	21
α-helix	435-436	2
β-strand	450	1	23
β-strand	453-454	2	24
α-helix	455-456	2
β-strand	463-467	5	25
β-strand	473-480	8	25
β-strand	484-487	4	25
α-helix	489-492	4
β-strand	493	1	26
α-helix	494-497	4
β-strand	508	1	26
α-helix	509-510	2
α-helix	511-513	3
β-strand	515-518	4	25
β-strand	522	1	27
β-strand	531-533	3	25
β-strand	535-540	6	25
β-strand	554-558	5	25
α-helix	561-564	4
α-helix	570-571	2
β-strand	572	1	24
α-helix	573-574	2
α-helix	577-579	3
β-strand	583-588	6	24
α-helix	593-595	3
α-helix	596-598	3
β-strand	600	1	27
β-strand	602-609	8	24
α-helix	610	1
α-helix	611-617	7
β-strand	629-632	4	24
β-strand	640	1	23
β-strand	649-653	5	24
β-strand	660-669	10	24
β-strand	679-683	5	24
α-helix	685-687	3
α-helix	688-694	7

Chain B: 20 helices, 41 β-strands

Element	Residues	Length	Sheet
β-strand	310-312	3	28
β-strand	324-329	6	28
β-strand	333-337	5	29
β-strand	340-342	3	29
β-strand	344-348	5	28
β-strand	349	1	30
β-strand	355	1	30
β-strand	361-364	4	29
α-helix	365	1
α-helix	370-372	3
β-strand	376-380	5	31
β-strand	392-397	6	31
α-helix	398	1
β-strand	402-404	3	32
α-helix	405-407	3
β-strand	411-414	4	31
β-strand	420-421	2	31
β-strand	422	1	33
β-strand	426	1	33
β-strand	432-434	3	32
α-helix	435-436	2
β-strand	450	1	34
β-strand	453-454	2	35
α-helix	455-456	2
β-strand	463-467	5	36
β-strand	473-480	8	36
β-strand	484-487	4	36
α-helix	489-492	4
β-strand	493	1	37
α-helix	494-497	4
β-strand	508	1	37
α-helix	509-510	2
α-helix	511-513	3
β-strand	515-518	4	36
β-strand	522	1	38
β-strand	531-533	3	36
β-strand	535-540	6	36
β-strand	545	1	39
β-strand	550	1	39
β-strand	554-558	5	36
β-strand	565	1	40
β-strand	568	1	40
α-helix	570-571	2
β-strand	572	1	35
α-helix	573-574	2
α-helix	577-579	3
β-strand	583-588	6	35
α-helix	593-595	3
α-helix	596-598	3
β-strand	600	1	38
β-strand	602-609	8	35
α-helix	610	1
α-helix	611-617	7
β-strand	629-632	4	35
β-strand	640	1	34
β-strand	649-653	5	35
α-helix	655-657	3
β-strand	660-669	10	35
β-strand	679-683	5	35
α-helix	685-687	3
α-helix	688-694	7

Chain C: 19 helices, 41 β-strands

Element	Residues	Length	Sheet
β-strand	300-301	2	1
α-helix	305-307	3
β-strand	310-312	3	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	345-348	4	2
β-strand	349	1	4
β-strand	355	1	4
β-strand	361-364	4	3
α-helix	365	1
α-helix	370-372	3
β-strand	376-380	5	5
β-strand	392-397	6	5
α-helix	398	1
β-strand	402-404	3	6
α-helix	405-407	3
β-strand	411-414	4	5
β-strand	420-421	2	5
β-strand	422	1	7
β-strand	426	1	7
β-strand	432-434	3	6
α-helix	435-436	2
β-strand	450	1	8
β-strand	453-454	2	9
α-helix	455-456	2
β-strand	463-467	5	10
β-strand	473-480	8	10
β-strand	484-487	4	10
α-helix	489-492	4
β-strand	493	1	11
α-helix	494-497	4
β-strand	508	1	11
α-helix	509-510	2
α-helix	511-513	3
β-strand	515-518	4	10
β-strand	522	1	12
β-strand	531-533	3	10
β-strand	535-540	6	10
β-strand	554-558	5	10
β-strand	565	1	13
β-strand	568	1	13
β-strand	572	1	9
α-helix	573-574	2
α-helix	577-579	3
β-strand	583-588	6	9
α-helix	593-595	3
α-helix	596-598	3
β-strand	600	1	12
β-strand	602-609	8	9
α-helix	610	1
α-helix	611-617	7
β-strand	629-632	4	9
β-strand	640	1	8
β-strand	649-653	5	9
β-strand	660-669	10	9
β-strand	679-683	5	9
α-helix	685-687	3
α-helix	688-694	7

Chain I: 5 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	13-16	4
β-strand	20-25	6	24
α-helix	27-29	3
α-helix	33-35	3
β-strand	36-48	13	41
β-strand	53-54	2	24
β-strand	55	1	42
β-strand	56-63	8	24
β-strand	70-83	14	24
β-strand	93-98	6	41
β-strand	99	1	42
α-helix	102-105	4
β-strand	106-108	3	41
β-strand	115-120	6	24
β-strand	124-132	9	41
β-strand	137-138	2	41
β-strand	140	1	35

Chain J: 5 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	13-16	4
β-strand	20-25	6	35
α-helix	27-29	3
α-helix	33-35	3
β-strand	36-48	13	41
β-strand	53-54	2	35
β-strand	55	1	43
β-strand	56-63	8	35
β-strand	70-83	14	35
β-strand	93-98	6	41
β-strand	99	1	43
α-helix	102-104	3
β-strand	106-108	3	41
β-strand	115-120	6	35
β-strand	124-132	9	41
β-strand	137-138	2	41
β-strand	140	1	24

Chain K: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4
α-helix	13-16	4
β-strand	20-25	6	9
α-helix	27-29	3
α-helix	33-35	3
β-strand	36-48	13	14
β-strand	53-54	2	9
β-strand	55	1	15
β-strand	56-63	8	9
β-strand	70-83	14	9
β-strand	93-98	6	14
β-strand	99	1	15
α-helix	102-104	3
β-strand	106-108	3	14
β-strand	115-120	6	9
β-strand	124-131	8	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mannan-binding lectin serine protease 1	A, B, C	protein	406	Homo sapiens	P48740 (AlphaFold model)
Ecotin	I, J, K	protein	162	Escherichia coli (strain K12)	P23827 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>7PQO_1 Mannan-binding lectin serine protease 1 (chains A, B, C)
ASMTGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDG
TWSNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYT
CSAQGVWMNKVLGRSLPTCLPVCGLPKFSRKLMARIFNGRPAQKGTTPWIAMLSHLNGQP
FCGGSLLGSSWIVTAAHCLHQSLDPKDPTLRDSDLLSPSDFKIILGKHWRLRSDENEQHL
GVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVSGWGKQF
LQRFPETLMEIEIPIVDHSTCQKAYAPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTL
NRERGQWYLVGTVSWGDDCGKKDRYGVYSYIHHNKDWIQRVTGVRN

Sequence of entity 2 (I, J, K), FASTA

>7PQO_2 Ecotin (chains I, J, K)
MKTILPAVLFAAFATTSAWAAESVQPLEKIAPYPQAEKGMKRQVIQLTPQEDESTLKVEL
LIGQTLEVDCNLHRLGGKLENKTLEGWGYDYYVFDKVSSPVSTRMACPDGKKEKKFVTAY
LGDAGMLRYNSKLPIVVYTPDNVDVKYRVWKAEEKIDNAVVR

Primary citation

Synergy of protease-binding sites within the ecotin homodimer is crucial for inhibition of MASP enzymes and for blocking lectin pathway activation. Nagy, Z.A., Heja, D., Bencze, D. et al. J Biol Chem (2022) 298:101985-101985. DOI 10.1016/j.jbc.2022.101985 · 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…
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
4AQB 4.2 Å, MBL-Ficolin Associated Protein-1, MAP-1 aka MAP44

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