1Q3X: Catalytic region of human MASP-2

Crystal structure of the catalytic region of human MASP-2. Determined by X-ray diffraction at 2.23 Å resolution. Released 3 Aug 2004.

Method: X-ray diffraction
Resolution: 2.23 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,232
Mol. weight: 72.2 kDa
Released: 3 Aug 2004

Explore 1Q3X in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1Q3X contains 23 α-helices and 54 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: 12 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	365	1	1
α-helix	369-371	3
β-strand	375-379	5	2
β-strand	387	1	1
β-strand	391-396	6	2
β-strand	401-404	4	3
β-strand	409-412	4	2
β-strand	418-420	3	2
α-helix	427-428	2
β-strand	429-432	4	3
β-strand	446	1	4
β-strand	449-450	2	5
α-helix	451-452	2
β-strand	459-462	4	6
β-strand	468-473	6	6
β-strand	477-480	4	6
α-helix	482-489	8
β-strand	496-499	4	6
β-strand	503	1	7
β-strand	510-519	10	6
β-strand	534-538	5	6
β-strand	545	1	8
β-strand	548	1	8
α-helix	550-551	2
β-strand	552	1	5
α-helix	553-554	2
α-helix	556-561	6
β-strand	567-572	6	5
β-strand	584	1	7
β-strand	586-593	8	5
α-helix	594	1
α-helix	595-601	7
α-helix	608	1
β-strand	616-619	4	5
β-strand	627	1	4
β-strand	636-641	6	5
β-strand	646-655	10	5
β-strand	667-671	5	5
α-helix	672-675	4
α-helix	676-685	10

Chain B: 11 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	369-371	3
β-strand	375-379	5	9
β-strand	391-396	6	9
β-strand	401-404	4	10
β-strand	409-411	3	9
β-strand	419-420	2	9
α-helix	427-428	2
β-strand	429-432	4	10
β-strand	446	1	11
β-strand	449-450	2	12
β-strand	459-462	4	13
β-strand	468-473	6	13
β-strand	477-480	4	13
α-helix	482-489	8
β-strand	496-499	4	13
β-strand	503	1	14
β-strand	510-519	10	13
β-strand	534-538	5	13
α-helix	541-544	4
β-strand	545	1	15
β-strand	548	1	15
α-helix	550-551	2
β-strand	552	1	12
α-helix	553-555	3
α-helix	556-561	6
β-strand	567-572	6	12
β-strand	584	1	14
β-strand	586-593	8	12
α-helix	595-601	7
α-helix	608	1
β-strand	616-619	4	12
β-strand	627	1	11
β-strand	636-641	6	12
β-strand	646-655	10	12
β-strand	667-671	5	12
α-helix	672-675	4
α-helix	676-685	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mannan-binding lectin serine protease 2	A, B	protein	328	Homo sapiens	O00187 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1Q3X_1 Mannan-binding lectin serine protease 2 (chains A, B)
ASMTIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTMKVNDGKYVCEADGFW
TSSKGEKSLPVCEPVCGLSARTTGGRIYGGQKAKPGDFPWQVLILGGTTAAGALLYDNWV
LTAAHAVYEQKHDASALDIRMGTLKRLSPHYTQAWSEAVFIHEGYTHDAGFDNDIALIKL
NNKVVINSNITPICLPRKEAESFMRTDDIGTASGWGLTQRGFLARNLMYVDIPIVDHQKC
TAAYEKPPYPRGSVTANMLCAGLESGGKDSCRGDSGGALVFLDSETERWFVGGIVSWGSM
NCGEAGQYGVYTKVINYIPWIENIISDF

Primary citation

The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions. Harmat, V., Gal, P., Kardos, J. et al. J Mol Biol (2004) 342:1533-1546. DOI 10.1016/j.jmb.2004.07.014 · PubMed

Other PDB entries of the same protein (UniProt O00187 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3TVJ 1.28 Å, Catalytic fragment of MASP-2 in complex with its specific inhibitor developed by…
9D40 1.76 Å, Crystal structure of the catalytic region of human MASP-2 with specific inhibitor Analog…
9D17 1.97 Å, Crystal structure of the catalytic region of human MASP-2 with specific inhibitor…
9D3Y 2.08 Å, Crystal structure of the catalytic region of human MASP-2 with specific inhibitor…
1ZJK 2.18 Å, Crystal structure of the zymogen catalytic region of human MASP-2
9D4D 2.36 Å, Crystal structure of the catalytic region of human MASP-2 with specific inhibitor…
7PQN 2.4 Å, Catalytic fragment of MASP-2 in complex with ecotin
1SZB 2.5 Å, Crystal structure of the human MBL-associated protein 19 (MAp19)
5JPM 3.75 Å, Structure of the complex of human complement C4 with MASP-2 rebuilt using iMDFF

Browse structure collections

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