Crystal structure of anti-lysozyme antibody. Determined by X-ray diffraction at 2.1 Å resolution. Released 19 Jan 2000.
Explore 1DQM in 3D Show helices and sheets RCSB PDB PDBe
1DQM contains 17 α-helices and 46 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 | 3 | 1 | 6 |
| β-strand | 6-7 | 2 | 7 |
| β-strand | 11-12 | 2 | 8 |
| β-strand | 18-23 | 6 | 7 |
| β-strand | 25 | 1 | 6 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-40 | 7 | 2 |
| β-strand | 44-51 | 8 | 2 |
| β-strand | 57-59 | 3 | 2 |
| α-helix | 61-63 | 3 | |
| β-strand | 67-72 | 6 | 7 |
| β-strand | 77-82 | 6 | 7 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-97 | 7 | 2 |
| β-strand | 103 | 1 | 2 |
| β-strand | 107-109 | 3 | 2 |
| β-strand | 110-111 | 2 | 8 |
| β-strand | 117 | 1 | 9 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 10 |
| α-helix | 125-127 | 3 | |
| β-strand | 135-145 | 11 | 10 |
| β-strand | 146 | 1 | 9 |
| β-strand | 151-155 | 4 | 11 |
| α-helix | 160-162 | 3 | |
| β-strand | 164 | 1 | 11 |
| β-strand | 169-171 | 3 | 10 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 10 |
| β-strand | 183-192 | 10 | 10 |
| α-helix | 193-196 | 3 | |
| β-strand | 204-210 | 6 | 11 |
| α-helix | 211-213 | 3 | |
| β-strand | 215-220 | 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 | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| α-helix | 50-52 | 3 | |
| β-strand | 53-54 | 2 | 2 |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 84-90 | 7 | 2 |
| β-strand | 97-98 | 2 | 2 |
| β-strand | 102-106 | 5 | 2 |
| β-strand | 111 | 1 | 3 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 144-150 | 7 | 5 |
| β-strand | 153-155 | 3 | 5 |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-186 | 4 | |
| β-strand | 191-198 | 8 | 5 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Anti-lysozyme antibody hyhel-63 (light chain) | L | protein | 214 | Mus musculus | P01837 (AlphaFold model) |
| Anti-lysozyme antibody hyhel-63 (heavy chain) | H | protein | 210 | Mus musculus | P01863 (AlphaFold model) |
>1DQM_1 ANTI-LYSOZYME ANTIBODY HYHEL-63 (LIGHT CHAIN) (chains L) DIVLTQSPATLSVTPGDSVSLSCRASQSISNNLHWYQQKSHESPRLLIKYASQSISGIPS RFSGSGSGTDFTLSINSVETEDFGMYFCQQSNSWPYTFGGGTKLEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1DQM_2 ANTI-LYSOZYME ANTIBODY HYHEL-63 (HEAVY CHAIN) (chains H) EVQLQESGPSLVKPSQTLSLTCSVTGDSVTSDYWSWIRKFPGNKLEYMGYISYSGSTYYH PSLKSRISITRDTSKNQYYLQLNSVTTEDTATYYCASWGGDVWGAGTTVTVSSAKTTAPS VYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSS VTVTSSTWPSQSITCNVAHPASSTKVDKKI
Three-dimensional structures of the free and antigen-bound Fab from monoclonal antilysozyme antibody HyHEL-63(,). Li, Y., Li, H., Smith-Gill, S.J. et al. Biochemistry (2000) 39:6296-6309. DOI 10.1021/bi000054l · 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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