The Structure Of The Complex Of The Fab Fragment Of The Esterolytic Antibody MS6-164 and A Transition-State Analog. Determined by X-ray diffraction at 2.1 Å resolution. Released 23 Sept 2003.
Explore 1MH5 in 3D Show helices and sheets RCSB PDB PDBe
1MH5 contains 20 α-helices and 87 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 | 4-5 | 2 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 27C | 1 | 3 |
| β-strand | 31 | 1 | 3 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-66 | 5 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 4 |
| β-strand | 114-118 | 5 | 5 |
| β-strand | 131-139 | 9 | 5 |
| β-strand | 140 | 1 | 4 |
| β-strand | 147-150 | 4 | 6 |
| β-strand | 153 | 1 | 6 |
| β-strand | 159-163 | 5 | 5 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-180 | 8 | 5 |
| β-strand | 192-195 | 4 | 6 |
| β-strand | 206-209 | 4 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 7 |
| β-strand | 9-12 | 4 | 8 |
| β-strand | 18-25 | 8 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 32-39 | 8 | 8 |
| β-strand | 46-52 | 7 | 8 |
| β-strand | 56-59 | 4 | 8 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 7 |
| β-strand | 77-82 | 6 | 7 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 8 |
| β-strand | 101-103 | 3 | 8 |
| β-strand | 107-111 | 5 | 8 |
| β-strand | 117 | 1 | 9 |
| β-strand | 139-142 | 4 | 10 |
| β-strand | 147 | 1 | 11 |
| β-strand | 148 | 1 | 9 |
| β-strand | 172-173 | 2 | 10 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 11 |
| β-strand | 185-186 | 2 | 11 |
| β-strand | 189-192 | 4 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 18 |
| β-strand | 9-12 | 4 | 19 |
| β-strand | 18-25 | 8 | 18 |
| α-helix | 29-31 | 3 | |
| β-strand | 32-39 | 8 | 19 |
| β-strand | 45-52 | 8 | 19 |
| β-strand | 56-59 | 4 | 19 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 18 |
| α-helix | 73-75 | 3 | |
| β-strand | 77-82 | 6 | 18 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-96 | 9 | 19 |
| β-strand | 101-103 | 3 | 19 |
| β-strand | 107-111 | 5 | 19 |
| α-helix | 115-116 | 2 | |
| β-strand | 117 | 1 | 20 |
| β-strand | 139-140 | 2 | 21 |
| β-strand | 147 | 1 | 22 |
| β-strand | 148 | 1 | 20 |
| β-strand | 153-158 | 4 | 23 |
| β-strand | 166 | 1 | 23 |
| β-strand | 169-173 | 4 | 21 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-179 | 3 | 22 |
| β-strand | 184-186 | 3 | 22 |
| β-strand | 189-192 | 4 | 21 |
| β-strand | 208-211 | 4 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 12 |
| β-strand | 10-13 | 4 | 13 |
| β-strand | 19-25 | 7 | 12 |
| β-strand | 27C | 1 | 14 |
| β-strand | 31 | 1 | 14 |
| β-strand | 33-38 | 6 | 13 |
| β-strand | 45-49 | 5 | 13 |
| β-strand | 53-54 | 2 | 13 |
| α-helix | 55 | 1 | |
| β-strand | 62-66 | 5 | 12 |
| β-strand | 70-75 | 6 | 12 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 13 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 13 |
| β-strand | 102-106 | 5 | 13 |
| β-strand | 111 | 1 | 15 |
| β-strand | 114-118 | 5 | 16 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 16 |
| β-strand | 140 | 1 | 15 |
| β-strand | 146-150 | 5 | 17 |
| β-strand | 153 | 1 | 17 |
| β-strand | 159-163 | 5 | 16 |
| β-strand | 173-182 | 10 | 16 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-196 | 6 | 17 |
| β-strand | 205-210 | 6 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin MS6-164 | A, L | protein | 219 | Mus musculus | P01837 (AlphaFold model) |
| Immunoglobulin MS6-164 | B, H | protein | 230 | Mus musculus | P01863 (AlphaFold model) |
>1MH5_1 IMMUNOGLOBULIN MS6-164 (chains A, L) DIVMTQAAPSVSVTPGESVSISCRSSKSLLHSNGNTYLYWFLQRPGQSPQLLIYRMSNLA SGVPDRFSGSGSGTAFTLRISRVEAEDVGVYYCLQHLEYPFTFGAGTKLELKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1MH5_2 IMMUNOGLOBULIN MS6-164 (chains B, H) QVQLQQPGAELVKPGASVKLSCKASGYTFTSNWINWVKQRPGQGLEWIGNIYPDSYRTNY NEKFKRKATLTVDTSSSTAYMQLSSLTSDDSAVYYCVRKHYSYDGVVYWGQGTLVTVSAA KTTAPSVYPLAPVCGDTSGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDL YTLSSSVTVTSSTWPSQSITCNVAHPASSTKVDKKIEPRGPTIKPCPPCK
| ID | Name | Formula | Copies |
|---|---|---|---|
| HAL | N-{[2-({[1-(4-carboxybutanoyl)amino]-2-phenylethyl}-hydroxyphosphinyl)oxy]acety… | C23 H29 N2 O7 P | 2 |
Water and common crystallization additives (SO4) are not listed.
High-resolution crystal structure of the Fab-fragments of a family of mouse catalytic antibodies with esterase activity. Ruzheinikov, S.N., Muranova, T.A., Sedelnikova, S.E. et al. J Mol Biol (2003) 332:423-435. DOI 10.1016/S0022-2836(03)00902-1 · PubMed
Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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