Complex of tissue inhibitor of metalloproteinase-1 (TIMP-1) mutant L34G with matrix metalloproteinase-3 catalytic domain (MMP-3cd). Determined by X-ray diffraction at 2.37 Å resolution. Released 15 May 2019.
Explore 6MAV in 3D Show helices and sheets RCSB PDB PDBe
6MAV contains 13 α-helices and 22 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 | 96-101 | 6 | 1 |
| α-helix | 110-125 | 16 | |
| β-strand | 131-135 | 5 | 1 |
| β-strand | 142-147 | 6 | 1 |
| β-strand | 163-167 | 5 | 1 |
| β-strand | 178-181 | 4 | 1 |
| β-strand | 186-187 | 2 | 2 |
| β-strand | 193-194 | 2 | 2 |
| α-helix | 195-207 | 13 | |
| α-helix | 209-211 | 3 | |
| β-strand | 222 | 1 | 1 |
| α-helix | 229-231 | 3 | |
| α-helix | 236-246 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-3 | 2 | 1 |
| α-helix | 5-7 | 3 | |
| α-helix | 8-14 | 7 | |
| β-strand | 17-23 | 7 | 3 |
| β-strand | 28-30 | 3 | 4 |
| β-strand | 35-39 | 5 | 4 |
| β-strand | 40-47 | 8 | 3 |
| β-strand | 60-64 | 5 | 4 |
| α-helix | 67-69 | 3 | |
| β-strand | 83-87 | 5 | 3 |
| β-strand | 88-90 | 3 | 4 |
| β-strand | 93-95 | 3 | 4 |
| β-strand | 102-104 | 3 | 3 |
| α-helix | 105-107 | 3 | |
| α-helix | 110-116 | 7 | |
| α-helix | 120-123 | 4 | |
| β-strand | 128-131 | 4 | 5 |
| β-strand | 144-147 | 4 | 5 |
| α-helix | 149-153 | 5 | |
| α-helix | 159-163 | 5 | |
| β-strand | 164-170 | 7 | 6 |
| β-strand | 173-178 | 6 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Stromelysin-1 | A | protein | 168 | Homo sapiens | P08254 (AlphaFold model) |
| Metalloproteinase inhibitor 1 | B | protein | 184 | Homo sapiens | P01033 (AlphaFold model) |
>6MAV_1 Stromelysin-1 (chains A) FRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADI MISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHE IGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPP
>6MAV_2 Metalloproteinase inhibitor 1 (chains B) CTCVPPHPQTAFCNSDLVIRAKFVGTPEVNQTTGYQRYEIKMTKMYKGFQALGDAADIRF VYTPAMESVCGYFHRSHNRSEEFLIAGKLQDGLLHITTCSFVAPWNSLSLAQRRGFTKTY TVGCEECTVFPCLSIPCKLQSGTHCLWTDQLLQGSEKGFQSRHLACLPREPGLCTWQSLR SQIA
Directed evolution of the metalloproteinase inhibitor TIMP-1 reveals that its N- and C-terminal domains cooperate in matrix metalloproteinase recognition. Raeeszadeh-Sarmazdeh, M., Greene, K.A., Sankaran, B. et al. J Biol Chem (2019) 294:9476-9488. DOI 10.1074/jbc.RA119.008321 · PubMed
Other PDB entries of the same protein (UniProt P08254 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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