4AQB: Mannan-binding lectin serine protease 1

MBL-Ficolin Associated Protein-1, MAP-1 aka MAP44. Determined by X-ray diffraction at 4.2 Å resolution. Released 8 Aug 2012.

Method: X-ray diffraction
Resolution: 4.2 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 2,914
Mol. weight: 43.36 kDa
Ligands: CA
Released: 8 Aug 2012

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

Secondary structure: helices and β-sheets

4AQB contains 11 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: 11 helices, 37 β-strands

Element	Residues	Length	Sheet
β-strand	23-25	3	1
β-strand	28-32	5	2
α-helix	39-41	3
β-strand	44-51	8	1
β-strand	56-66	11	2
α-helix	71-73	3
β-strand	77-81	5	1
β-strand	86-90	5	1
β-strand	93	1	2
α-helix	105-106	2
β-strand	107-108	2	2
β-strand	113-120	8	1
β-strand	130-139	10	2
α-helix	142-144	3
α-helix	146-148	3
β-strand	156-160	5	3
β-strand	163-167	5	3
β-strand	173-174	2	4
β-strand	181-182	2	4
β-strand	190	1	5
β-strand	194-198	5	6
α-helix	205-207	3
β-strand	211-217	7	5
β-strand	223-228	6	6
β-strand	233	1	7
β-strand	234	1	8
β-strand	246-251	6	5
β-strand	254-259	6	5
β-strand	261	1	8
α-helix	264-267	4
β-strand	268-269	2	6
β-strand	274-280	7	5
β-strand	289	1	7
β-strand	291-297	7	6
α-helix	299	1
β-strand	300-301	2	9
α-helix	302-304	3
α-helix	306-307	2
β-strand	310-313	4	10
β-strand	319-320	2	9
β-strand	324-329	6	10
β-strand	333-337	5	11
β-strand	340-342	3	11
β-strand	344-348	5	10
β-strand	349	1	12
β-strand	355	1	12
α-helix	358-360	3
β-strand	361-364	4	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mannan-binding lectin serine protease 1	A	protein	361	HOMO SAPIENS	P48740 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4AQB_1 MANNAN-BINDING LECTIN SERINE PROTEASE 1 (chains A)
HTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVK
VETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVD
VDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSDNLFTQRTGVITS
PDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPF
CGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKY
FFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDGTWSNKIPTCKKNEIDLESELKSEQVT
E

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	6

Primary citation

Crystal Structure and Functional Characterization of the Complement Regulator Mannose-Binding Lectin (Mbl)/Ficolin-Associated Protein-1 (Map-1). Skjoedt, M.O., Roversi, P., Hummelshoj, T. et al. J Biol Chem (2012) 287:32913. DOI 10.1074/JBC.M112.386680 · 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
7PQO 3.39 Å, Catalytic fragment of MASP-1 in complex with P1 site mutant ecotin

Browse structure collections

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