Crystal structure of the Fab M75. Determined by X-ray diffraction at 2.1 Å resolution. Released 13 Nov 2007.
Explore 2HKH in 3D Show helices and sheets RCSB PDB PDBe
2HKH contains 13 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 | 5-7 | 3 | 7 |
| β-strand | 10-12 | 3 | 8 |
| β-strand | 18-23 | 6 | 7 |
| β-strand | 34-39 | 6 | 8 |
| β-strand | 45-51 | 7 | 8 |
| α-helix | 54-56 | 3 | |
| β-strand | 60-62 | 3 | 8 |
| β-strand | 70-75 | 6 | 7 |
| β-strand | 80-85 | 6 | 7 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-100 | 7 | 8 |
| β-strand | 108-109 | 2 | 8 |
| β-strand | 113-117 | 5 | 8 |
| β-strand | 123 | 1 | 9 |
| α-helix | 124-125 | 2 | |
| β-strand | 126-130 | 5 | 10 |
| β-strand | 141-151 | 11 | 10 |
| β-strand | 152 | 1 | 9 |
| β-strand | 157-160 | 4 | 11 |
| β-strand | 169-177 | 9 | 10 |
| β-strand | 180-190 | 11 | 10 |
| α-helix | 191-193 | 3 | |
| β-strand | 200-205 | 6 | 11 |
| α-helix | 206-208 | 3 | |
| β-strand | 210-215 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 30 | 1 | 3 |
| β-strand | 36 | 1 | 3 |
| β-strand | 38-43 | 6 | 2 |
| α-helix | 48-49 | 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 | 4 |
| β-strand | 119-123 | 5 | 5 |
| α-helix | 124-126 | 3 | |
| α-helix | 127-131 | 5 | |
| β-strand | 134-144 | 11 | 5 |
| β-strand | 145 | 1 | 4 |
| β-strand | 150-155 | 6 | 6 |
| β-strand | 158-160 | 3 | 6 |
| β-strand | 164-168 | 5 | 5 |
| α-helix | 169-172 | 4 | |
| β-strand | 178-187 | 10 | 5 |
| α-helix | 188-191 | 4 | |
| β-strand | 196-203 | 8 | 6 |
| β-strand | 206-215 | 10 | 6 |
| α-helix | 216-218 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin Light chain Fab fragment | L | protein | 219 | Mus musculus | P01631 (AlphaFold model) |
| Immunoglobulin Heavy chain Fab fragment | H | protein | 218 | Mus musculus |
>2HKH_1 Immunoglobulin Light chain Fab fragment (chains L) DVVMTQTPLSLPVSLGDQASISCRSSQSLVHSNGNTYLHWYLQKPGQSPNLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYFCSQSTHVPFTFGSGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>2HKH_2 Immunoglobulin Heavy chain Fab fragment (chains H) EVQVVESGGGLVQPKGSLKLSCVVSGSTLNNYAMNWVRQAPGKGLEWVARIRSKSNNYAT YYADSVKDRFTISRDDSQSMIYLQMNNLKTEDTAMYYCVTYGNHPFAYWGQGTLVTVSAA KTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSGL YTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLEP
Stabilization of antibody structure upon association to a human carbonic anhydrase IX epitope studied by X-ray crystallography, microcalorimetry, and molecular dynamics simulations. Kral, V., Mader, P., Collard, R. et al. Proteins (2008) 71:1275-1287. DOI 10.1002/prot.21821 · PubMed
Other PDB entries of the same protein (UniProt P01631 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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