1BQQ: MT1-mmp--timp-2 complex

Crystal structure of the MT1-mmp--timp-2 complex. Determined by X-ray diffraction at 2.75 Å resolution. Released 18 Aug 1999.

Method: X-ray diffraction
Resolution: 2.75 Å
Organisms: Homo sapiens, Bos taurus
Chains: 2
Atoms: 3,150
Mol. weight: 40.54 kDa
Ligands: ZN, CA
Released: 18 Aug 1999

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

Secondary structure: helices and β-sheets

1BQQ contains 12 α-helices and 27 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 M: 6 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	123-125	3	1
β-strand	127-128	2	2
α-helix	137-154	18
β-strand	158-160	3	1
β-strand	178-182	5	2
β-strand	198-202	5	2
α-helix	203-204	2
β-strand	213-216	4	2
β-strand	222	1	3
β-strand	232	1	3
α-helix	233-243	11
β-strand	260	1	2
α-helix	273-276	4
α-helix	279	1
α-helix	280-285	6

Chain T: 6 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	1002-1003	2	2
α-helix	1008-1014	7
β-strand	1017-1022	6	4
β-strand	1023	1	5
β-strand	1029-1030	2	6
β-strand	1042-1045	4	6
β-strand	1047	1	5
β-strand	1051-1054	4	4
β-strand	1063-1065	3	6
β-strand	1083-1088	6	4
β-strand	1089-1090	2	6
β-strand	1096-1097	2	6
β-strand	1104-1106	3	4
α-helix	1107-1109	3
α-helix	1112-1115	4
α-helix	1121-1124	4
α-helix	1125-1127	3
β-strand	1129	1	7
β-strand	1132	1	8
β-strand	1145	1	7
β-strand	1148	1	8
α-helix	1160-1163	4
β-strand	1166-1169	4	9
β-strand	1175-1178	4	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Membrane-type matrix metalloproteinase	M	protein	174	Homo sapiens	P50281 (AlphaFold model)
Metalloproteinase inhibitor 2	T	protein	184	Bos taurus	P16368 (AlphaFold model)

Sequence of entity 1 (M), FASTA

>1BQQ_1 MEMBRANE-TYPE MATRIX METALLOPROTEINASE (chains M)
IQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEK
QADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDI
FLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGES

Sequence of entity 2 (T), FASTA

>1BQQ_2 METALLOPROTEINASE INHIBITOR 2 (chains T)
CSCSPVHPQQAFCNADIVIRAKAVNKKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDQDI
EFIYTAPAAAVCGVSLDIGGKKEYLIAGKAEGNGNMHITLCDFIVPWDTLSATQKKSLNH
RYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRG
AAPP

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2
CA	Calcium ion	Ca	2

Primary citation

Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor. Fernandez-Catalan, C., Bode, W., Huber, R. et al. EMBO J (1998) 17:5238-5248. DOI 10.1093/emboj/17.17.5238 · 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
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
6CM1 MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs

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