6CM1: MT1-MMP HPX Domain with Blade 2 Loop

MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs. Determined by solution NMR. Released 12 Dec 2018.

Method: Solution NMR
Organism: Homo sapiens
Chains: 3
Atoms: 15,173
Mol. weight: 221.02 kDa
Ligands: PX4
Released: 12 Dec 2018

Explore 6CM1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6CM1 contains 20 α-helices and 24 β-strands across 3 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: 10 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	318-320	3
β-strand	325-329	5	1
β-strand	332-337	6	1
β-strand	340-344	5	1
β-strand	349	1	1
α-helix	350	1
α-helix	354	1
β-strand	355-356	2	1
α-helix	357-360	4
β-strand	370-373	4	2
β-strand	379-383	5	2
β-strand	386-390	5	2
β-strand	395	1	2
β-strand	397	1	3
β-strand	399	1	3
β-strand	401-402	2	2
α-helix	403-405	3
β-strand	417-420	4	4
β-strand	427-431	5	4
β-strand	434-439	6	4
β-strand	444-445	2	4
α-helix	446	1
β-strand	451-452	2	4
α-helix	453-455	3
β-strand	457	1	5
α-helix	459-460	2
β-strand	465-468	4	6
β-strand	474-479	6	6
β-strand	482-487	6	6
β-strand	492	1	5
β-strand	493	1	6
α-helix	494	1
β-strand	499-500	2	6
α-helix	501-504	4

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	56-63	8
α-helix	65-168	104
α-helix	173-264	92

Chain C: 7 helices, 0 β-strands

Element	Residues	Length
α-helix	57-97	41
α-helix	101-104	4
α-helix	107-118	12
α-helix	120-223	104
α-helix	225-228	4
α-helix	230-258	29
α-helix	262-264	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Matrix metalloproteinase-14	A	protein	196	Homo sapiens	P50281 (AlphaFold model)
Apolipoprotein A-I	B, C	protein	211	Homo sapiens	P02647 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6CM1_1 Matrix metalloproteinase-14 (chains A)
PNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERK
DGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKY
YRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEP
GYPKSALRDWMGCPSG

Sequence of entity 2 (B, C), FASTA

>6CM1_2 Apolipoprotein A-I (chains B, C)
STFSKLREQLGPVTQEFWDNLEKETEGLRQEMSKDLEEVKAKVQPYLDDFQKKWQEEMEL
YRQKVEPYLDDFQKKWQEEMELYRQKVEPLRAELQEGARQKLHELQEKLSPLGEEMRDRA
RAHVDALRTHLAPYSDELRQRLAARLEALKENGGARLAEYHAKATEHLSTLSEKAKPALE
DLRQGLLPVLESFKVSFLSALEEYTKKLNTQ

Ligands and cofactors

ID	Name	Formula	Copies
PX4	1,2-dimyristoyl-sn-glycero-3-phosphocholine	C36 H73 N O8 P	218

Water and common crystallization additives (CL, NA) are not listed.

Primary citation

MT1-MMP Binds Membranes by Opposite Tips of Its beta Propeller to Position It for Pericellular Proteolysis. Marcink, T.C., Simoncic, J.A., An, B. et al. Structure (2019) 27:281-292.e6. DOI 10.1016/j.str.2018.10.008 · PubMed

Other PDB entries of the same protein (UniProt P50281 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3C7X 1.7 Å, Hemopexin-like domain of matrix metalloproteinase 14
4P3C 1.94 Å, MT1-MMP:Fab complex (Form I)
4P3D 1.95 Å, MT1-MMP:Fab complex (Form II)
3MA2 2.05 Å, Complex membrane type-1 matrix metalloproteinase (MT1-MMP) with tissue inhibitor of…
5H0U 2.24 Å, Crystal structure of the catalytic domain of membrane type 1 matrix metalloproteinase
4QXU 2.3 Å, Novel Inhibition Mechanism of Membrane Metalloprotease by an Exosite-Swiveling…
3X23 2.4 Å, Radixin complex
1BQQ 2.75 Å, Crystal structure of the MT1-mmp--timp-2 complex
1BUV 2.75 Å, Crystal structure of the MT1-mmp-timp-2 complex
2MQS Transient Collagen Triple Helix Binding to a Key Metalloproteinase in Invasion and…
6CLZ MT1-MMP HPX domain with Blade 4 Loop Bound to Nanodiscs

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