4QXU: Anti_MT1-MMP Light chain

Novel Inhibition Mechanism of Membrane Metalloprotease by an Exosite-Swiveling Conformational antibody. Determined by X-ray diffraction at 2.3 Å resolution. Released 17 Dec 2014.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Mus musculus, Homo sapiens
Chains: 3
Atoms: 3,458
Mol. weight: 50.64 kDa
Released: 17 Dec 2014

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

Secondary structure: helices and β-sheets

4QXU contains 17 α-helices and 43 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 H: 9 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	6
β-strand	11-12	2	7
β-strand	18-25	8	6
α-helix	29-31	3
β-strand	34-39	6	8
β-strand	45-51	7	8
β-strand	58-60	3	8
α-helix	62-64	3
β-strand	68-73	6	6
α-helix	74-76	3
β-strand	78-83	6	6
α-helix	88-90	3
β-strand	92-100	9	8
β-strand	103-108	6	8
β-strand	112-114	3	8
β-strand	115-116	2	7
β-strand	122	1	9
β-strand	125-129	5	10
α-helix	130-132	3
β-strand	140-150	11	10
β-strand	151	1	9
β-strand	156-159	4	11
α-helix	160-162	3
β-strand	168-170	3	10
α-helix	171-173	3
β-strand	174-176	3	10
β-strand	179-189	11	10
β-strand	199-204	6	11
α-helix	205-207	3
β-strand	209-214	6	11
α-helix	217-219	3

Chain L: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-13	4	2
β-strand	19-25	7	1
β-strand	38-43	6	2
β-strand	50-54	5	2
β-strand	58-59	2	2
β-strand	67-72	6	1
β-strand	75-80	6	1
α-helix	85-87	3
β-strand	89-95	7	2
α-helix	101	1
β-strand	102-103	2	2
β-strand	107-111	5	2
β-strand	116	1	3
α-helix	117-118	2
β-strand	119-123	5	4
α-helix	124-126	3
α-helix	127-131	5
β-strand	134-144	11	4
β-strand	145	1	3
β-strand	150-155	6	5
β-strand	158-160	3	5
β-strand	164-168	5	4
α-helix	169-172	4
β-strand	178-187	10	4
α-helix	188-191	4
β-strand	196-202	7	5
β-strand	210-215	6	5
α-helix	216-218	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
anti_MT1-MMP Light chain	L	protein	219	Mus musculus
anti_MT1-MMP Heavy chain	H	protein	231	Mus musculus
Matrix metalloproteinase-14	K	protein	11	Homo sapiens	P50281 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>4QXU_1 anti_MT1-MMP Light chain (chains L)
DVLMTQTPLSLPVGLGDQASISCRSSQSIVHSNGNTYLEWYLQKPGQSPKLLIYKVSNRF
SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHAPYTFGGGTKLEIKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM
SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC

Sequence of entity 2 (H), FASTA

>4QXU_2 anti_MT1-MMP Heavy chain (chains H)
EVKLVESGGGLVKPGGSLKLSCAASGFIFSNYAMSWVRQTPEKRLEWVATISGGGRNIYS
LDSVKGRFTFFRDNARNTLYLQMSSLRSEDTAMYFCSRENYGSSFTYWGQGTLVTVSSAK
TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDCAAALEHHHHHH

Sequence of entity 3 (K), FASTA

>4QXU_3 Matrix metalloproteinase-14 (chains K)
AEPWTVRNEDL

Primary citation

Inhibition mechanism of membrane metalloprotease by an exosite-swiveling conformational antibody. Udi, Y., Grossman, M., Solomonov, I. et al. Structure (2015) 23:104-115. DOI 10.1016/j.str.2014.10.012 · 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
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
6CM1 MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs

Browse structure collections

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