Orthorhombic form of IgG1 Fab fragment (in complex with antigenic tubulin peptide) sharing same Fv as IgA. Determined by X-ray diffraction at 2.2 Å resolution. Released 15 Feb 2012.
Explore 3QNZ in 3D Show helices and sheets RCSB PDB PDBe
3QNZ contains 20 α-helices and 45 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 | 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 |
| β-strand | 50-54 | 5 | 2 |
| β-strand | 58-59 | 2 | 2 |
| α-helix | 60 | 1 | |
| 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 |
| α-helix | 112 | 1 | |
| β-strand | 116 | 1 | 4 |
| α-helix | 117-118 | 2 | |
| 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 | 158-159 | 2 | 6 |
| α-helix | 160 | 1 | |
| β-strand | 164-168 | 5 | 5 |
| α-helix | 169-172 | 4 | |
| β-strand | 178-187 | 10 | 5 |
| α-helix | 188-193 | 6 | |
| β-strand | 196-202 | 7 | 6 |
| β-strand | 210-215 | 6 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 7 |
| β-strand | 10-12 | 3 | 8 |
| β-strand | 18-24 | 7 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 33-39 | 7 | 8 |
| β-strand | 46-51 | 6 | 8 |
| α-helix | 54-56 | 3 | |
| β-strand | 60-62 | 3 | 8 |
| α-helix | 64-66 | 3 | |
| β-strand | 70-75 | 6 | 7 |
| β-strand | 80-85 | 6 | 7 |
| α-helix | 90-92 | 3 | |
| β-strand | 94-101 | 8 | 8 |
| β-strand | 109 | 1 | 8 |
| β-strand | 113-117 | 5 | 8 |
| α-helix | 121-122 | 2 | |
| 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 |
| α-helix | 161-163 | 3 | |
| β-strand | 165 | 1 | 11 |
| β-strand | 169-171 | 3 | 10 |
| α-helix | 172-174 | 3 | |
| β-strand | 175-176 | 2 | 10 |
| β-strand | 182-191 | 10 | 10 |
| α-helix | 192-194 | 3 | |
| β-strand | 201-206 | 6 | 11 |
| α-helix | 207-209 | 3 | |
| β-strand | 211-216 | 6 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fab fragment of IMMUNOGLOBULIN G1 LIGHT CHAIN | A | protein | 219 | Homo sapiens | |
| Fab fragment of IMMUNOGLOBULIN G1 HEAVY CHAIN | B | protein | 220 | Homo sapiens | |
| peptide from Tubulin beta chain | C | protein | 10 | P07437 (AlphaFold model) |
>3QNZ_1 Fab fragment of IMMUNOGLOBULIN G1 LIGHT CHAIN (chains A) DIVMTQSPLSLSVTPGEPASISCRSSQSLLRRDGHNDLEWYLQKPGQSPQPLIYLGSTRA SGVPDRFSGSGSGTDFTLKIIRVEAEDAGTYYCMQNKQTPLTFGQGTRLEIKRTVAAPSV FIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSL SSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>3QNZ_2 Fab fragment of IMMUNOGLOBULIN G1 HEAVY CHAIN (chains B) EVQLVESGGGLVQPGGSLKLSCAASGFTLSGSNVHWVRQASGKGLEWVGRIKRNAESDAT AYAASMRGRLTISRDDSKNTAFLQMNSLKSDDTAMYYCVIRGDVYNRQWGQGTLVTVSSA STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPK
>3QNZ_3 peptide from Tubulin beta chain (chains C) TAEEEEDFGE
Structure of a human IgA1 Fab fragment at 1.55 angstrom resolution: potential effect of the constant domains on antigen-affinity modulation. Correa, A., Trajtenberg, F., Obal, G. et al. Acta Crystallogr D Biol Crystallogr (2013) 69:388-397. DOI 10.1107/S0907444912048664 · PubMed
Other PDB entries of the same protein (UniProt P07437 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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