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.
Explore 4QXU in 3D Show helices and sheets RCSB PDB PDBe
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.
| 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 |
| 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 |
| 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) |
>4QXU_1 anti_MT1-MMP Light chain (chains L) DVLMTQTPLSLPVGLGDQASISCRSSQSIVHSNGNTYLEWYLQKPGQSPKLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHAPYTFGGGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>4QXU_2 anti_MT1-MMP Heavy chain (chains H) EVKLVESGGGLVKPGGSLKLSCAASGFIFSNYAMSWVRQTPEKRLEWVATISGGGRNIYS LDSVKGRFTFFRDNARNTLYLQMSSLRSEDTAMYFCSRENYGSSFTYWGQGTLVTVSSAK TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY TLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDCAAALEHHHHHH
>4QXU_3 Matrix metalloproteinase-14 (chains K) AEPWTVRNEDL
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:
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