MT1-MMP:Fab complex (Form I). Determined by X-ray diffraction at 1.94 Å resolution. Released 17 Dec 2014.
Explore 4P3C in 3D Show helices and sheets RCSB PDB PDBe
4P3C contains 16 α-helices and 48 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 | 1 |
| β-strand | 11-12 | 2 | 2 |
| β-strand | 18-25 | 8 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 3 |
| β-strand | 45-51 | 7 | 3 |
| β-strand | 58-60 | 3 | 3 |
| α-helix | 62-64 | 3 | |
| β-strand | 68-73 | 6 | 1 |
| α-helix | 74-76 | 3 | |
| β-strand | 78-83 | 6 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-100 | 9 | 3 |
| β-strand | 103-108 | 6 | 3 |
| β-strand | 112-114 | 3 | 3 |
| β-strand | 115-116 | 2 | 2 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 4 |
| α-helix | 123-124 | 2 | |
| β-strand | 125-129 | 5 | 5 |
| β-strand | 140-150 | 11 | 5 |
| β-strand | 151 | 1 | 4 |
| β-strand | 156-159 | 4 | 6 |
| α-helix | 160-162 | 3 | |
| β-strand | 164 | 1 | 6 |
| β-strand | 168-170 | 3 | 5 |
| α-helix | 171-173 | 3 | |
| β-strand | 174-176 | 3 | 5 |
| β-strand | 179-189 | 11 | 5 |
| α-helix | 190-192 | 3 | |
| β-strand | 199-204 | 6 | 6 |
| α-helix | 205-207 | 3 | |
| β-strand | 209-214 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 7 |
| β-strand | 10-13 | 4 | 8 |
| β-strand | 19-25 | 7 | 7 |
| β-strand | 30 | 1 | 9 |
| β-strand | 36 | 1 | 9 |
| β-strand | 38-43 | 6 | 8 |
| β-strand | 49-54 | 6 | 8 |
| β-strand | 58-59 | 2 | 8 |
| α-helix | 60 | 1 | |
| β-strand | 67-72 | 6 | 7 |
| β-strand | 75-80 | 6 | 7 |
| α-helix | 85-87 | 3 | |
| β-strand | 89-95 | 7 | 8 |
| α-helix | 101 | 1 | |
| β-strand | 102-103 | 2 | 8 |
| β-strand | 107-111 | 5 | 8 |
| β-strand | 117 | 1 | 10 |
| β-strand | 120-124 | 5 | 11 |
| α-helix | 125-127 | 3 | |
| α-helix | 128-132 | 5 | |
| β-strand | 135-145 | 11 | 11 |
| β-strand | 146 | 1 | 10 |
| β-strand | 150-156 | 7 | 12 |
| β-strand | 159-161 | 3 | 12 |
| β-strand | 165-170 | 6 | 11 |
| β-strand | 173 | 1 | 13 |
| β-strand | 176 | 1 | 13 |
| β-strand | 179-188 | 10 | 11 |
| α-helix | 189-192 | 4 | |
| β-strand | 197-204 | 8 | 12 |
| β-strand | 211-216 | 6 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heavy Chain Fab fragment of antibody LEM-2/15 | H | protein | 218 | Mus musculus | |
| Light Chain Fab fragment of antibody LEM-2/15 | L | protein | 218 | Mus musculus | |
| Matrix metalloproteinase-14 | M | protein | 13 | Homo sapiens | P50281 (AlphaFold model) |
>4P3C_1 Heavy Chain Fab fragment of antibody LEM-2/15 (chains H) EVKLVESGGGLVKPGGSLKLSCAASGFIFSNYAMSWVRQTPEKRLEWVATISGGGRNIYS LDSVKGRFTFFRDNARNTLYLQMSSLRSEDTAMYFCSRENYGSSFTYWGQGTLVTVSSAK TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY TLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPR
>4P3C_2 Light Chain Fab fragment of antibody LEM-2/15 (chains L) DVLMTQTPLSLPVGLGDQASISCRSSQSIVHSNGNTYLEWYLQKPGQSPKLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHAPYTFGGGTKLEIKRAADAAPT VSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYS MSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRN
>4P3C_3 Matrix metalloproteinase-14 (chains M) FDSAEPWTVRNED
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
Water and common crystallization additives (ACT, EDO, EPE, CL) are not listed.
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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