4KKD: Mannan-binding lectin serine protease 1

The X-ray crystal structure of Mannose-binding lectin-associated serine proteinase-3 reveals the structural basis for enzyme inactivity associated with the 3MC syndrome. Determined by X-ray diffraction at 2.6 Å resolution. Released 3 Jul 2013.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,403
Mol. weight: 96.08 kDa
Released: 3 Jul 2013

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

Secondary structure: helices and β-sheets

4KKD contains 33 α-helices and 79 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: 14 helices, 40 β-strands

Element	Residues	Length	Sheet
α-helix	299	1
β-strand	300-301	2	1
α-helix	305-307	3
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	420-421	2	6
β-strand	422	1	8
β-strand	426	1	8
β-strand	432-434	3	7
β-strand	455	1	9
β-strand	464-471	8	10
β-strand	478-488	11	10
β-strand	491-494	4	10
α-helix	496-499	4
β-strand	500	1	11
α-helix	501-502	2
β-strand	510	1	11
α-helix	511-512	2
α-helix	513-515	3
β-strand	516-520	5	10
β-strand	524	1	12
β-strand	532-541	10	10
β-strand	546	1	13
β-strand	551	1	13
β-strand	555-559	5	10
α-helix	571-572	2
β-strand	573	1	9
α-helix	574-576	3
β-strand	587-592	6	9
β-strand	616	1	12
β-strand	618-625	8	9
α-helix	627-633	7
β-strand	647-650	4	9
β-strand	667-671	5	9
β-strand	678-686	9	9
β-strand	699-703	5	9
α-helix	704-706	3
α-helix	708-715	8

Chain B: 19 helices, 39 β-strands

Element	Residues	Length	Sheet
α-helix	299	1
β-strand	300-301	2	14
α-helix	302-303	2
α-helix	305-307	3
β-strand	310-313	4	15
β-strand	319-320	2	14
β-strand	324-329	6	15
β-strand	333-337	5	16
β-strand	340-342	3	16
β-strand	344-348	5	15
β-strand	349	1	17
β-strand	355	1	17
β-strand	361-364	4	16
α-helix	365	1
β-strand	366	1	18
α-helix	370-372	3
β-strand	376-380	5	19
β-strand	388	1	18
β-strand	392-397	6	19
β-strand	402-404	3	20
β-strand	411-414	4	19
β-strand	420-421	2	19
β-strand	422	1	21
β-strand	426	1	21
α-helix	429-430	2
β-strand	432-434	3	20
β-strand	454-455	2	22
α-helix	456-457	2
β-strand	464-471	8	23
β-strand	478-486	9	23
β-strand	491-494	4	23
α-helix	496-499	4
β-strand	500	1	24
β-strand	510	1	24
α-helix	511-512	2
α-helix	513-515	3
β-strand	516-520	5	23
β-strand	524	1	25
α-helix	528-530	3
β-strand	532-541	10	23
β-strand	555-559	5	23
α-helix	563-565	3
β-strand	566	1	26
β-strand	569	1	26
β-strand	573	1	22
α-helix	574-576	3
α-helix	583	1
β-strand	587-594	8	22
β-strand	613-625	13	22
α-helix	626	1
α-helix	627-635	9
β-strand	647-650	4	22
β-strand	667-672	6	22
β-strand	677-686	10	22
α-helix	691	1
β-strand	699-703	5	22
α-helix	704-706	3
α-helix	708-715	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mannan-binding lectin serine protease 1	A, B	protein	433	Homo sapiens	P48740 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4KKD_1 Mannan-binding lectin serine protease 1 (chains A, B)
MAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDGTW
SNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYTCS
AQGVWMNKVLGRSLPTCLPECGQPSRSLPSLVQRIIGGRNAEPGLFPWQALIVVEDTSRV
PNDKWFGSGALLSASWILTAAHVLRSQRRDTTVIPVSKEHVTVYLGLHDVRDKSGAVNSS
AARVVLHPDFNIQNYNHDIALVQLQEPVPLGPHVMPVCLPRLEPEGPAPHMLGLVAGWGI
SNPNVTVDEIISSGTRTLSDVLQYVKLPVVPHAECKTSYESRSGNYSVTENMFCAGYYEG
GKDTCLGDSGEAFVIFDDLSQRWVVQGLVSWGGPEECGSKQVYGVYTKVSNYVDWVWEQM
GLPQSVVEPQVER

Primary citation

The X-ray Crystal Structure of Mannose-binding Lectin-associated Serine Proteinase-3 Reveals the Structural Basis for Enzyme Inactivity Associated with the Carnevale, Mingarelli, Malpuech, and Michels (3MC) Syndrome. Yongqing, T., Wilmann, P.G., Reeve, S.B. et al. J Biol Chem (2013) 288:22399-22407. DOI 10.1074/jbc.M113.483875 · 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
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

Browse structure collections

About this viewer

MolViewer shows 4KKD directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.