potassium channel KcsA-Fab complex in high concentration of Tl+. Determined by X-ray diffraction at 1.9 Å resolution. Released 25 Nov 2003.
Explore 1R3J in 3D Show helices and sheets RCSB PDB PDBe
1R3J contains 17 α-helices and 43 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 | 4-5 | 2 | 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 |
| 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 | 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 |
| β-strand | 114-118 | 5 | 4 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-125 | 4 | |
| β-strand | 129-139 | 11 | 4 |
| β-strand | 140 | 1 | 3 |
| β-strand | 145-150 | 6 | 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 | 183-187 | 5 | |
| β-strand | 191-197 | 7 | 5 |
| α-helix | 204 | 1 | |
| β-strand | 205-210 | 6 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-5 | 2 | 6 |
| β-strand | 9-12 | 4 | 7 |
| β-strand | 18-24 | 7 | 6 |
| β-strand | 33-39 | 7 | 7 |
| β-strand | 46-52 | 7 | 7 |
| β-strand | 57-60 | 4 | 7 |
| β-strand | 68-73 | 6 | 6 |
| β-strand | 78-83 | 6 | 6 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-99 | 8 | 7 |
| β-strand | 107-108 | 2 | 7 |
| β-strand | 112-116 | 5 | 7 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 8 |
| α-helix | 123-124 | 2 | |
| β-strand | 125-129 | 5 | 9 |
| β-strand | 140-150 | 11 | 9 |
| β-strand | 151 | 1 | 8 |
| β-strand | 156-159 | 4 | 10 |
| α-helix | 160-162 | 3 | |
| β-strand | 164 | 1 | 10 |
| β-strand | 168-170 | 3 | 9 |
| α-helix | 171-173 | 3 | |
| β-strand | 174-175 | 2 | 9 |
| β-strand | 180-189 | 10 | 9 |
| α-helix | 190-192 | 3 | |
| β-strand | 199-204 | 6 | 10 |
| α-helix | 205-207 | 3 | |
| β-strand | 209-214 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 24-51 | 28 | |
| α-helix | 62-73 | 12 | |
| α-helix | 86-121 | 36 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Antibody Fab fragment light chain | A | protein | 212 | Mus musculus | P01837 (AlphaFold model) |
| Antibody Fab fragment heavy chain | B | protein | 219 | Mus musculus | P01868 (AlphaFold model) |
| Voltage-gated potassium channel | C | protein | 124 | Streptomyces lividans | P0A334 (AlphaFold model) |
>1R3J_1 Antibody Fab fragment light chain (chains A) DILLTQSPAILSVSPGERVSFSCRASQSIGTDIHWYQQRTNGSPRLLIKYASESISGIPS RFSGSGSGTDFTLSINSVESEDIANYYCQQSNRWPFTFGSGTKLEIKRADAAPTVSIFPP SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT LTKDEYERHNSYTCEATHKTSTSPIVKSFNRN
>1R3J_2 Antibody Fab fragment heavy chain (chains B) QVQLQQPGAELVKPGASVKLSCKASGYTFTSDWIHWVKQRPGHGLEWIGEIIPSYGRANY NEKIQKKATLTADKSSSTAFMQLSSLTSEDSAVYYCARERGDGYFAVWGAGTTVTVSSAK TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY TLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRD
>1R3J_3 Voltage-gated potassium channel (chains C) MAPMLSGLLARLVKLLLGRHGSALHWRAAGAATVLLVIVLLAGSYLAVLAERGAPGAQLI TYPRALWWSVETATTVGYGDLYPVTLWGRCVAVVVMVAGITSFGLVTAALATWFVGREQE RRGH
The occupancy of ions in the K+ selectivity filter: Charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates. Zhou, Y., MacKinnon, R. J Mol Biol (2003) 333:965-975. DOI 10.1016/j.jmb.2003.09.022 · 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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