1DSX: KV1.2 T1 domain, residues 33-119, T46V mutant
KV1.2 T1 domain, residues 33-119, T46V mutant. Determined by X-ray diffraction at 1.6 Å resolution. Released 20 Sept 2000.
- Method
- X-ray diffraction
- Resolution
- 1.6 Å
- Organism
- Rattus norvegicus
- Chains
- 8
- Atoms
- 6,495
- Mol. weight
- 83.97 kDa
- Released
- 20 Sept 2000
Explore 1DSX in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1DSX contains 38 α-helices and 32 β-strands across 8 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.
Chain A: 4 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 34-39 | 6 | 1 |
| β-strand | 42-47 | 6 | 1 |
| α-helix | 48-52 | 5 | |
| α-helix | 62-66 | 5 | |
| β-strand | 69-70 | 2 | 1 |
| β-strand | 75-78 | 4 | 1 |
| α-helix | 85-93 | 9 | |
| α-helix | 106-116 | 11 | |
Chain B: 4 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 34-39 | 6 | 2 |
| β-strand | 42-47 | 6 | 2 |
| α-helix | 48-52 | 5 | |
| α-helix | 62-66 | 5 | |
| β-strand | 69-70 | 2 | 2 |
| β-strand | 75-78 | 4 | 2 |
| α-helix | 85-93 | 9 | |
| α-helix | 106-115 | 10 | |
Chains C and D: 5 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 34-39 | 6 | 3 |
| β-strand | 42-47 | 6 | 3 |
| α-helix | 48-52 | 5 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 3 |
| β-strand | 75-78 | 4 | 3 |
| α-helix | 82-93 | 12 | |
| α-helix | 106-115 | 10 | |
Chain E: 5 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 34-39 | 6 | 5 |
| β-strand | 42-47 | 6 | 5 |
| α-helix | 48-51 | 4 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 5 |
| β-strand | 75-78 | 4 | 5 |
| α-helix | 85-93 | 9 | |
| α-helix | 106-116 | 11 | |
Chain F: 5 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 34-39 | 6 | 6 |
| β-strand | 42-47 | 6 | 6 |
| α-helix | 48-52 | 5 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 6 |
| β-strand | 75-78 | 4 | 6 |
| α-helix | 85-93 | 9 | |
| α-helix | 106-116 | 11 | |
Chain G: 5 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 34-39 | 6 | 7 |
| β-strand | 42-47 | 6 | 7 |
| α-helix | 48-52 | 5 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 7 |
| β-strand | 75-78 | 4 | 7 |
| α-helix | 83-94 | 12 | |
| α-helix | 106-116 | 11 | |
Chain H: 5 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 34-39 | 6 | 8 |
| β-strand | 42-47 | 6 | 8 |
| α-helix | 48-52 | 5 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-68 | 3 | |
| β-strand | 69-70 | 2 | 8 |
| β-strand | 75-78 | 4 | 8 |
| α-helix | 83-93 | 11 | |
| α-helix | 106-116 | 11 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein (KV1.2 voltage-gated potassium channel) | A, B, C, D, E, F, G, H | protein | 87 | Rattus norvegicus | P63142 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>1DSX_1 PROTEIN (KV1.2 VOLTAGE-GATED POTASSIUM CHANNEL) (chains A, B, C, D, E, F, G, H)
ERVVINISGLRFEVQLKTLAQFPETLLGDPKKRMRYFDPLRNEYFFDRNRPSFDAILYYY
QSGGRLRRPVNVPLDIFSEEIRFYELG
Primary citation
The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel. Minor, D.L., Lin, Y.F., Mobley, B.C. et al. Cell (2000) 102:657-670. DOI 10.1016/S0092-8674(00)00088-X · PubMed
Other PDB entries of the same protein (UniProt P63142 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1QDV 1.6 Å, N-terminal domain, voltage-gated potassium channel KV1.2 residues 33-131
- 1QDW 2.1 Å, N-terminal domain, voltage-gated potassium channel KV1.2 residues 33-119
- 4JTA 2.5 Å, Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Charybdotoxin
- 4JTD 2.54 Å, Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Lys27Met mutant of…
- 8VCH 2.55 Å, Voltage gated potassium ion channel Kv1.2 W366F, C-type inactivated
- 4JTC 2.56 Å, Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Charybdotoxin in Cs+
- 2A79 2.9 Å, Mammalian Shaker Kv1.2 potassium channel- beta subunit complex
- 3LNM 2.9 Å, F233W mutant of the Kv2.1 paddle-Kv1.2 chimera channel
- 3LUT 2.9 Å, A Structural Model for the Full-length Shaker Potassium Channel Kv1.2
- 6EBL 3.0 Å, The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs, cytosolic…
- 7SIZ 3.1 Å, C-type inactivation in a voltage gated K+ channel
- 8VC4 3.17 Å, Voltage gated potassium ion channel Kv1.2 in Sodium
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