Anti-blood group A Fv. Determined by X-ray diffraction at 2.2 Å resolution. Released 9 Jan 2002.
Explore 1JV5 in 3D Show helices and sheets RCSB PDB PDBe
1JV5 contains 5 α-helices and 22 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 | 4-5 | 2 | 1 |
| β-strand | 10-13 | 4 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 33-38 | 6 | 2 |
| β-strand | 44-49 | 6 | 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 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 304-305 | 2 | 3 |
| β-strand | 309-312 | 4 | 2 |
| β-strand | 318-324 | 7 | 3 |
| α-helix | 329-331 | 3 | |
| β-strand | 334-339 | 6 | 2 |
| β-strand | 345-351 | 7 | 2 |
| β-strand | 358-360 | 3 | 2 |
| β-strand | 368-373 | 6 | 3 |
| β-strand | 378-383 | 6 | 3 |
| α-helix | 388-390 | 3 | |
| β-strand | 392-400 | 9 | 2 |
| β-strand | 403-408 | 6 | 2 |
| β-strand | 412-416 | 5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ig kappa chain precursor V region | A | protein | 107 | Homo sapiens | P01594 (AlphaFold model) |
| Ig chain heavy chain precursor V region | B | protein | 117 | Homo sapiens |
>1JV5_1 Ig kappa chain precursor V region (chains A) DIQMTQTTSSLSASLGDRVTISCRASQDINNYLNWYQQKPDGTVKLLIHYTSRLHSGVPS RFSGSGSGTDYSLTISNLEQEDIATYFCQQGNTLPWTFGGGTKLEIK
>1JV5_2 Ig chain heavy chain precursor V region (chains B) QVQLQQPGAELVKPGTSVKLSCKASGYNFTSYWINWVKLRPGQGLEWIGDIYPGSGITNY NEKFKSKATLTVDTSSSTAYMQLSSLASEDSALYYCAGQYGNLWFAYWGQGTLVTVS
Structure of an anti-blood group A Fv and improvement of its binding affinity without loss of specificity. Thomas, R., Patenaude, S.I., MacKenzie, C.R. et al. J Biol Chem (2002) 277:2059-2064. DOI 10.1074/jbc.M104364200 · PubMed
Other PDB entries of the same protein (UniProt P01594 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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