1ZJK: Zymogen catalytic region of human MASP-2

Crystal structure of the zymogen catalytic region of human MASP-2. Determined by X-ray diffraction at 2.18 Å resolution. Released 26 Jul 2005.

Method: X-ray diffraction
Resolution: 2.18 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,994
Mol. weight: 44.03 kDa
Released: 26 Jul 2005

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

Secondary structure: helices and β-sheets

1ZJK contains 17 α-helices and 37 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: 17 helices, 37 β-strands

Element	Residues	Length	Sheet
α-helix	299	1
β-strand	300	1	1
α-helix	301-302	2
α-helix	304-306	3
β-strand	309-311	3	2
β-strand	318	1	1
β-strand	323-325	3	3
β-strand	326-328	3	2
α-helix	329	1
β-strand	332-336	5	4
β-strand	339-340	2	4
β-strand	345-347	3	3
β-strand	348	1	5
β-strand	354	1	5
α-helix	357-359	3
β-strand	360-363	4	4
β-strand	365	1	6
α-helix	369-371	3
β-strand	375-379	5	7
β-strand	387	1	6
β-strand	391-396	6	7
β-strand	401-404	4	8
β-strand	409-412	4	7
β-strand	418-420	3	7
β-strand	429-432	4	8
α-helix	433	1
β-strand	449-450	2	9
α-helix	451-452	2
β-strand	459-464	6	10
β-strand	468-473	6	10
β-strand	477-480	4	10
α-helix	482-485	4
α-helix	486-488	3
β-strand	495-499	5	10
β-strand	503	1	11
β-strand	510-519	10	10
β-strand	534-538	5	10
α-helix	541-544	4
β-strand	545	1	12
β-strand	548	1	12
α-helix	550-551	2
β-strand	552	1	9
α-helix	553-554	2
α-helix	556-561	6
β-strand	567-572	6	9
β-strand	584	1	11
β-strand	586-593	8	9
α-helix	595-601	7
β-strand	616-619	4	9
β-strand	636-641	6	9
β-strand	646-656	11	9
β-strand	667-671	5	9
α-helix	672-675	4
α-helix	676-683	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mannan-binding lectin serine protease 2	A	protein	403	Homo sapiens	O00187 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1ZJK_1 Mannan-binding lectin serine protease 2 (chains A)
ASMTGWKIHYTSTAHACPYPMAPPNGHVSPVQAKYILKDSFSIFCETGYELLQGHLPLKS
FTAVCQKDGSWDRPMPACSIVDCGPPDDLPSGRVEYITGPGVTTYKAVIQYSCEETFYTM
KVNDGKYVCEADGFWTSSKGEKSLPVCEPVCGLSARTTGGQIYGGQKAKPGDFPWQVLIL
GGTTAAGALLYDNWVLTAAHAVYEQKHDASALDIRMGTLKRLSPHYTQAWSEAVFIHEGY
THDAGFDNDIALIKLNNKVVINSNITPICLPRKEAESFMRTDDIGTASGWGLTQRGFLAR
NLMYVDIPIVDHQKCTAAYEKPPYPRGSVTANMLCAGLESGGKDSCRGDSGGALVFLDSE
TERWFVGGIVSWGSMNCGEAGQYGVYTKVINYIPWIENIISDF

Primary citation

A True Autoactivating Enzyme: Structural insight into mannose-binding lectin-associated serine protease-2 activations. Gal, P., Harmat, V., Kocsis, A. et al. J Biol Chem (2005) 280:33435-33444. DOI 10.1074/jbc.M506051200 · 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…
1Q3X 2.23 Å, Crystal structure of the 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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