Crystal structure of the FAB fragment of a human monoclonal IgM cold agglutinin. Determined by X-ray diffraction at 2.83 Å resolution. Released 14 Sept 2000.
Explore 1QLR in 3D Show helices and sheets RCSB PDB PDBe
1QLR contains 24 α-helices and 86 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 | 4-7 | 4 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| α-helix | 28-29 | 2 | |
| α-helix | 30-31 | 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 | 62-67 | 6 | 1 |
| β-strand | 70-75 | 6 | 1 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 2 |
| α-helix | 96 | 1 | |
| 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 | 145-150 | 6 | 5 |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 164-167 | 4 | |
| β-strand | 173-182 | 10 | 4 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-197 | 7 | 5 |
| β-strand | 205-210 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 6 |
| β-strand | 11-12 | 2 | 7 |
| β-strand | 18-25 | 8 | 6 |
| β-strand | 34-39 | 6 | 8 |
| β-strand | 46-51 | 6 | 8 |
| β-strand | 57-59 | 3 | 8 |
| α-helix | 64-66 | 3 | |
| β-strand | 67-72 | 6 | 6 |
| β-strand | 77-82 | 6 | 6 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-97 | 7 | 8 |
| β-strand | 109-110 | 2 | 8 |
| β-strand | 114-116 | 3 | 8 |
| β-strand | 117-118 | 2 | 7 |
| β-strand | 124 | 1 | 9 |
| β-strand | 127-131 | 5 | 10 |
| β-strand | 145-153 | 9 | 10 |
| β-strand | 154 | 1 | 9 |
| β-strand | 159-164 | 6 | 11 |
| β-strand | 169 | 1 | 11 |
| β-strand | 173-175 | 3 | 10 |
| β-strand | 179-181 | 3 | 10 |
| β-strand | 184-192 | 9 | 10 |
| β-strand | 205-211 | 7 | 11 |
| β-strand | 217-222 | 6 | 11 |
| α-helix | 223-224 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 12 |
| β-strand | 10-13 | 4 | 13 |
| β-strand | 19-25 | 7 | 12 |
| α-helix | 28-29 | 2 | |
| α-helix | 30-31 | 3 | |
| β-strand | 33-38 | 6 | 13 |
| β-strand | 45-49 | 5 | 13 |
| β-strand | 53-54 | 2 | 13 |
| α-helix | 55 | 1 | |
| β-strand | 62-67 | 6 | 12 |
| β-strand | 70-75 | 6 | 12 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 13 |
| α-helix | 96 | 1 | |
| β-strand | 97-98 | 2 | 13 |
| β-strand | 102-106 | 5 | 13 |
| β-strand | 111 | 1 | 14 |
| α-helix | 112-113 | 2 | |
| β-strand | 114-118 | 5 | 15 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-126 | 5 | |
| β-strand | 129-139 | 11 | 15 |
| β-strand | 140 | 1 | 14 |
| β-strand | 145-150 | 6 | 16 |
| β-strand | 159-163 | 5 | 15 |
| β-strand | 173-182 | 10 | 15 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-197 | 7 | 16 |
| β-strand | 205-210 | 6 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 17 |
| β-strand | 11-12 | 2 | 18 |
| β-strand | 18-25 | 8 | 17 |
| β-strand | 34-39 | 6 | 19 |
| β-strand | 46-51 | 6 | 19 |
| β-strand | 57-59 | 3 | 19 |
| α-helix | 64-66 | 3 | |
| β-strand | 67-72 | 6 | 17 |
| β-strand | 77-82 | 6 | 17 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-97 | 7 | 19 |
| β-strand | 109-110 | 2 | 19 |
| β-strand | 114-116 | 3 | 19 |
| β-strand | 117-118 | 2 | 18 |
| β-strand | 124 | 1 | 20 |
| β-strand | 127-131 | 5 | 21 |
| β-strand | 145-153 | 9 | 21 |
| β-strand | 154 | 1 | 20 |
| β-strand | 159-163 | 5 | 22 |
| β-strand | 169 | 1 | 22 |
| β-strand | 173-175 | 3 | 21 |
| β-strand | 179-181 | 3 | 21 |
| β-strand | 184-192 | 9 | 21 |
| β-strand | 206-211 | 6 | 22 |
| β-strand | 217-221 | 5 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| IgM kappa chain V-III (kau cold agglutinin) | A, C | protein | 215 | HOMO SAPIENS | Q6PJF2 (AlphaFold model) |
| IgM FAB region IV-J(H4)-C (kau cold agglutinin) | B, D | protein | 232 | HOMO SAPIENS | P01871 (AlphaFold model) |
>1QLR_1 IGM KAPPA CHAIN V-III (KAU COLD AGGLUTININ) (chains A, C) EIVLTQSPATLSLSPGERATLSCGASQSVSSNYLAWYQQKPGQAPRLLIYDASSRATGIP DRFSGSGSGTDFTLTISRLEPEDFAVYYCQQYGSSPLTFGGGTKVEIKRTVAAPSVFIFP PSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>1QLR_2 IGM FAB REGION IV-J(H4)-C (KAU COLD AGGLUTININ) (chains B, D) EVQLQQWGAGLLKPSETLSLTCAVYGGSFSDYYWSWIRQPPGKGLEWIGEINHSGSTNYN PSLKSRVTISVDTSKNQFSLKLSSVTAADTAVYYCARPPHDTSGHYWNYWGQGTLVTVSS GSASAPTLFPLVSCENSPSDTSSVAVGCLAQDFLPDSITFSWKYKNNSDISSTRGFPSVL RGGKYAATSQVLLPSKDVMQGTDEHVVCKVQHPNGNKEKNVPLPVIAELPPK
Three-dimensional structure of the Fab from a human IgM cold agglutinin. Cauerhff, A., Braden, B.C., Carvalho, J.G. et al. J Immunol (2000) 165:6422-6428. DOI 10.4049/jimmunol.165.11.6422 · PubMed
Other PDB entries of the same protein (UniProt Q6PJF2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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