Anti HIV1 protease FAB complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 31 Dec 1997.
Explore 1MF2 in 3D Show helices and sheets RCSB PDB PDBe
1MF2 contains 22 α-helices and 93 β-strands across 4 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 | 8 |
| β-strand | 10-12 | 3 | 9 |
| β-strand | 18-25 | 8 | 8 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-40 | 8 | 9 |
| β-strand | 44-51 | 8 | 9 |
| β-strand | 57-59 | 3 | 9 |
| β-strand | 68-72 | 5 | 8 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 8 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-98 | 11 | 9 |
| α-helix | 100D | 1 | |
| β-strand | 100E-103 | 7 | 9 |
| β-strand | 107-111 | 5 | 9 |
| α-helix | 114-116 | 3 | |
| β-strand | 117 | 1 | 10 |
| β-strand | 120-124 | 5 | 11 |
| β-strand | 130-140 | 11 | 11 |
| β-strand | 141 | 1 | 10 |
| β-strand | 146-149 | 4 | 12 |
| α-helix | 150-152 | 3 | |
| β-strand | 154 | 1 | 12 |
| β-strand | 158-160 | 3 | 11 |
| α-helix | 161-163 | 3 | |
| β-strand | 164-165 | 2 | 11 |
| β-strand | 170-179 | 10 | 11 |
| α-helix | 182-185 | 4 | |
| β-strand | 189-194 | 6 | 12 |
| α-helix | 195-197 | 3 | |
| β-strand | 199-204 | 6 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10 | 1 | 2 |
| β-strand | 13 | 1 | 3 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 27C-27D | 2 | 4 |
| β-strand | 30-31 | 2 | 4 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| β-strand | 84-90 | 7 | 2 |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-104 | 3 | 2 |
| β-strand | 106 | 1 | 3 |
| β-strand | 111 | 1 | 5 |
| β-strand | 114-118 | 5 | 6 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 6 |
| β-strand | 140 | 1 | 5 |
| β-strand | 145-150 | 6 | 7 |
| β-strand | 153-154 | 2 | 7 |
| β-strand | 159-163 | 5 | 6 |
| β-strand | 173-182 | 10 | 6 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 7 |
| β-strand | 205-210 | 6 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 13 |
| β-strand | 10 | 1 | 14 |
| β-strand | 13 | 1 | 15 |
| β-strand | 19-25 | 7 | 13 |
| β-strand | 27C-27D | 2 | 16 |
| β-strand | 30-31 | 2 | 16 |
| β-strand | 33-38 | 6 | 14 |
| β-strand | 45-49 | 5 | 14 |
| β-strand | 53-54 | 2 | 14 |
| β-strand | 62-67 | 6 | 13 |
| β-strand | 70-75 | 6 | 13 |
| β-strand | 84-90 | 7 | 14 |
| β-strand | 97-98 | 2 | 14 |
| β-strand | 102-104 | 3 | 14 |
| β-strand | 106 | 1 | 15 |
| β-strand | 111 | 1 | 17 |
| β-strand | 114-118 | 5 | 18 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 18 |
| β-strand | 140 | 1 | 17 |
| β-strand | 144-150 | 7 | 19 |
| β-strand | 153-154 | 2 | 19 |
| β-strand | 159-164 | 6 | 18 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-182 | 10 | 18 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-198 | 8 | 19 |
| β-strand | 205-210 | 6 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 20 |
| β-strand | 10-12 | 3 | 21 |
| β-strand | 18-25 | 8 | 20 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-40 | 8 | 21 |
| β-strand | 44-51 | 8 | 21 |
| β-strand | 57-59 | 3 | 21 |
| β-strand | 68-72 | 5 | 20 |
| β-strand | 77-82 | 6 | 20 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-98 | 11 | 21 |
| β-strand | 100E-103 | 7 | 21 |
| β-strand | 107-111 | 5 | 21 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 22 |
| β-strand | 120-124 | 5 | 23 |
| β-strand | 130-140 | 11 | 23 |
| β-strand | 141 | 1 | 22 |
| β-strand | 146-149 | 4 | 24 |
| α-helix | 150-152 | 3 | |
| β-strand | 158-160 | 3 | 23 |
| α-helix | 161-163 | 3 | |
| β-strand | 164-166 | 3 | 23 |
| β-strand | 169-179 | 11 | 23 |
| β-strand | 189-194 | 6 | 24 |
| α-helix | 195-197 | 3 | |
| β-strand | 199-204 | 6 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Monoclonal antibody F11.2.32 | L, M | protein | 215 | Mus musculus | P01654 (AlphaFold model) |
| Monoclonal antibody F11.2.32 | H, N | protein | 226 | Mus musculus | P01868 (AlphaFold model) |
>1MF2_1 MONOCLONAL ANTIBODY F11.2.32 (chains L, M) DTVLTQSPASLAVSLGQRATISCRASESVDYYGKSFMNWFQQKPGQPPKLLIYAASNQGS GVPARFSGSGSGTDFSLHIHPMEEDDSAMYFCQQSKEVPWTFGGGTKLEIKRADAAPTVS IFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMS STLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNR
>1MF2_2 MONOCLONAL ANTIBODY F11.2.32 (chains H, N) DVQLVESGGGLVQPGGSRKLSCAASGFTFMRFGMHWVRQAPEKGLEWVAYISSGSSTIYY ADTVKGRFTISRDNPKNTLFLQMTSLRSEDTALYYCARSGGIERYDGTYYVMDYWGQGTS VTVSSAKTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPA VLQSDLYTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRD
Three-dimensional structure of an Fab-peptide complex: structural basis of HIV-1 protease inhibition by a monoclonal antibody. Lescar, J., Stouracova, R., Riottot, M.M. et al. J Mol Biol (1997) 267:1207-1222. DOI 10.1006/jmbi.1997.0950 · PubMed
Other PDB entries of the same protein (UniProt P01654 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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