Crystal structure of the anti-lysozyme antibody hyhel-63 complexed with hen egg white lysozyme. Determined by X-ray diffraction at 2.0 Å resolution. Released 19 Jan 2000.
Explore 1DQJ in 3D Show helices and sheets RCSB PDB PDBe
1DQJ contains 21 α-helices and 55 β-strands across 3 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 | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 15 | 1 | 3 |
| β-strand | 17 | 1 | 3 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 45-49 | 5 | 2 |
| β-strand | 53-54 | 2 | 2 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 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 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 5 |
| β-strand | 140 | 1 | 4 |
| β-strand | 145-150 | 6 | 6 |
| β-strand | 153-155 | 3 | 6 |
| β-strand | 159-163 | 5 | 5 |
| α-helix | 164-165 | 2 | |
| α-helix | 167 | 1 | |
| β-strand | 173-182 | 10 | 5 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-197 | 7 | 6 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 7 |
| β-strand | 11-12 | 2 | 8 |
| β-strand | 18-25 | 8 | 7 |
| β-strand | 34-39 | 6 | 9 |
| β-strand | 45-51 | 7 | 9 |
| β-strand | 57-59 | 3 | 9 |
| β-strand | 67-72 | 6 | 7 |
| β-strand | 77-82 | 6 | 7 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-97 | 7 | 9 |
| β-strand | 103 | 1 | 9 |
| β-strand | 107-109 | 3 | 9 |
| β-strand | 110-111 | 2 | 8 |
| β-strand | 117 | 1 | 10 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-124 | 5 | 11 |
| β-strand | 135-145 | 11 | 11 |
| β-strand | 146 | 1 | 10 |
| β-strand | 151-155 | 4 | 12 |
| α-helix | 160-162 | 3 | |
| β-strand | 164 | 1 | 12 |
| β-strand | 169-171 | 3 | 11 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-177 | 3 | 11 |
| β-strand | 182-192 | 11 | 11 |
| β-strand | 204-210 | 6 | 12 |
| α-helix | 211-213 | 3 | |
| β-strand | 215-220 | 6 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 13 |
| α-helix | 5-14 | 10 | |
| β-strand | 20 | 1 | 14 |
| β-strand | 23 | 1 | 14 |
| α-helix | 25-36 | 12 | |
| β-strand | 39 | 1 | 13 |
| β-strand | 43-45 | 3 | 15 |
| β-strand | 51-53 | 3 | 15 |
| β-strand | 58-59 | 2 | 15 |
| β-strand | 65 | 1 | 16 |
| β-strand | 79 | 1 | 16 |
| α-helix | 80-83 | 4 | |
| α-helix | 89-98 | 10 | |
| α-helix | 104-107 | 4 | |
| α-helix | 109-114 | 6 | |
| α-helix | 120-123 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Anti-lysozyme antibody hyhel-63 (light chain) | A | protein | 214 | Mus musculus | P01837 (AlphaFold model) |
| Anti-lysozyme antibody hyhel-63 (heavy chain) | B | protein | 210 | Mus musculus | P01865 (AlphaFold model) |
| Lysozyme | C | protein | 129 | Gallus gallus | P00698 (AlphaFold model) |
>1DQJ_1 ANTI-LYSOZYME ANTIBODY HYHEL-63 (LIGHT CHAIN) (chains A) DIVLTQSPATLSVTPGDSVSLSCRASQSISNNLHWYQQKSHESPRLLIKYASQSISGIPS RFSGSGSGTDFTLSINSVETEDFGMYFCQQSNSWPYTFGGGTKLEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1DQJ_2 ANTI-LYSOZYME ANTIBODY HYHEL-63 (HEAVY CHAIN) (chains B) EVQLQESGPSLVKPSQTLSLTCSVTGDSVTSDYWSWIRKFPGNKLEYMGYISYSGSTYYH PSLKSRISITRDTSKNQYYLQLNSVTTEDTATYYCASWGGDVWGAGTTVTVSSAKTTAPS VYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSS VTVTSSTWPSQSITCNVAHPASSTKVDKKI
>1DQJ_3 LYSOZYME (chains C) KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINS RWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDV QAWIRGCRL
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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