Crystal structure of an immunogen specific anti-mannopyranoside monoclonal antibody Fab fragment. Determined by X-ray diffraction at 2.8 Å resolution. Released 19 Aug 2008.
Explore 2V7H in 3D Show helices and sheets RCSB PDB PDBe
2V7H contains 19 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 | 4-6 | 3 | 1 |
| β-strand | 10-14 | 5 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 44-48 | 5 | 2 |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| β-strand | 85-90 | 6 | 2 |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 103-107 | 5 | 2 |
| β-strand | 111 | 1 | 3 |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-150 | 6 | 5 |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 165-167 | 3 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-197 | 7 | 5 |
| β-strand | 205-210 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-5 | 3 | 6 |
| β-strand | 11-12 | 2 | 7 |
| β-strand | 18-25 | 8 | 6 |
| β-strand | 34-40 | 7 | 8 |
| β-strand | 44-51 | 8 | 8 |
| β-strand | 59 | 1 | 8 |
| β-strand | 68-71 | 4 | 6 |
| β-strand | 78-83 | 6 | 6 |
| β-strand | 92-99 | 8 | 8 |
| α-helix | 100 | 1 | |
| β-strand | 108-111 | 4 | 8 |
| β-strand | 115-117 | 3 | 8 |
| β-strand | 118-119 | 2 | 7 |
| β-strand | 125 | 1 | 9 |
| α-helix | 126-127 | 2 | |
| β-strand | 128-132 | 5 | 10 |
| β-strand | 143-153 | 11 | 10 |
| β-strand | 154 | 1 | 9 |
| β-strand | 159-162 | 4 | 11 |
| β-strand | 167 | 1 | 11 |
| β-strand | 171-173 | 3 | 10 |
| β-strand | 177-178 | 2 | 10 |
| β-strand | 183-192 | 10 | 10 |
| β-strand | 202-207 | 6 | 11 |
| α-helix | 208-210 | 3 | |
| β-strand | 212-217 | 6 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 20 |
| β-strand | 11-12 | 2 | 21 |
| β-strand | 18-25 | 8 | 20 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-40 | 8 | 22 |
| β-strand | 44-51 | 8 | 22 |
| β-strand | 58-60 | 3 | 22 |
| β-strand | 65 | 1 | 23 |
| β-strand | 68 | 1 | 23 |
| β-strand | 70-71 | 2 | 20 |
| β-strand | 78-83 | 6 | 20 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 22 |
| β-strand | 108-111 | 4 | 22 |
| β-strand | 115-117 | 3 | 22 |
| β-strand | 118-119 | 2 | 21 |
| α-helix | 126-127 | 2 | |
| β-strand | 128-132 | 5 | 24 |
| β-strand | 144-146 | 3 | 25 |
| β-strand | 147-153 | 7 | 24 |
| β-strand | 159-162 | 4 | 26 |
| α-helix | 163-165 | 3 | |
| β-strand | 167 | 1 | 26 |
| β-strand | 171-173 | 3 | 25 |
| α-helix | 174-176 | 3 | |
| β-strand | 177-178 | 2 | 24 |
| β-strand | 183-186 | 4 | 24 |
| β-strand | 187-191 | 5 | 25 |
| α-helix | 195-198 | 4 | |
| α-helix | 200 | 1 | |
| β-strand | 201-207 | 7 | 26 |
| α-helix | 208-210 | 3 | |
| β-strand | 212-218 | 7 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 12 |
| β-strand | 10-13 | 4 | 13 |
| β-strand | 19-25 | 7 | 12 |
| β-strand | 33-39 | 7 | 13 |
| β-strand | 43-48 | 6 | 13 |
| β-strand | 49 | 1 | 14 |
| β-strand | 54 | 1 | 14 |
| β-strand | 64-67 | 4 | 12 |
| β-strand | 70-75 | 6 | 12 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 13 |
| β-strand | 98 | 1 | 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 | 122-125 | 4 | |
| β-strand | 129-132 | 4 | 17 |
| β-strand | 133-139 | 7 | 16 |
| β-strand | 140 | 1 | 15 |
| β-strand | 144-150 | 7 | 18 |
| β-strand | 159-160 | 2 | 17 |
| β-strand | 163 | 1 | 16 |
| β-strand | 173-176 | 4 | 16 |
| β-strand | 178-182 | 5 | 17 |
| α-helix | 183-186 | 4 | |
| β-strand | 192-198 | 7 | 18 |
| β-strand | 199 | 1 | 19 |
| β-strand | 201 | 1 | 19 |
| β-strand | 205-209 | 5 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Monoclonal antibody | A, L | protein | 214 | MUS MUSCULUS | P01647 (AlphaFold model), P01837 (AlphaFold model) |
| Monoclonal antibody | B, H | protein | 220 | MUS MUSCULUS |
>2V7H_1 MONOCLONAL ANTIBODY (chains A, L) DIQMTQTTSSLSASLGDRVTISCRASQDINNYLNWYQQKPDGTVKILIYYTSNLHSGVPS RFSGSGSGTDYSLTISNLEQEDIATYFCQQGNTLPRTFGGGTKLEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSARQNGVLNSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>2V7H_2 MONOCLONAL ANTIBODY (chains B, H) QAQLQQSGAELMKPGASVKISCKATGYTFSNYWIDWIKQRPGHGLEWIGEILPGSGSTNY NEKFRGKATFTADTSSNTAYMQLSSLTSEDSAVYYCTRRGYWAYDFDYWGQGTTLTVSSA KTTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDL YTLSSSVTVPSSPRPSETVTCNVAHPASSTKVDKKIVPRD
Role of Antibody Paratope Conformational Flexibility in the Manifestation of Molecular Mimicry. Krishnan, L., Sahni, G., Kaur, K.J. et al. Biophys J (2008) 94:1367. DOI 10.1529/BIOPHYSJ.107.108654 · PubMed
Other PDB entries of the same protein (UniProt P01647 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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