4JTD
Crystal structure of Kv1.2-2.1 paddle chimera channel in complex with Lys27Met mutant of Charybdotoxin
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0002244 | biological_process | hematopoietic progenitor cell differentiation |
A | 0004033 | molecular_function | aldo-keto reductase (NADPH) activity |
A | 0005249 | molecular_function | voltage-gated potassium channel activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005874 | cellular_component | microtubule |
A | 0005886 | cellular_component | plasma membrane |
A | 0006813 | biological_process | potassium ion transport |
A | 0008076 | cellular_component | voltage-gated potassium channel complex |
A | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
A | 0014069 | cellular_component | postsynaptic density |
A | 0015459 | molecular_function | potassium channel regulator activity |
A | 0016020 | cellular_component | membrane |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0030424 | cellular_component | axon |
A | 0034705 | cellular_component | potassium channel complex |
A | 0043005 | cellular_component | neuron projection |
A | 0043194 | cellular_component | axon initial segment |
A | 0043679 | cellular_component | axon terminus |
A | 0044224 | cellular_component | juxtaparanode region of axon |
A | 0044325 | molecular_function | transmembrane transporter binding |
A | 0044877 | molecular_function | protein-containing complex binding |
A | 0045202 | cellular_component | synapse |
A | 0045445 | biological_process | myoblast differentiation |
A | 0050905 | biological_process | neuromuscular process |
A | 0055085 | biological_process | transmembrane transport |
A | 0055114 | biological_process | obsolete oxidation-reduction process |
A | 0070995 | biological_process | NADPH oxidation |
A | 0071805 | biological_process | potassium ion transmembrane transport |
A | 0098839 | cellular_component | postsynaptic density membrane |
A | 0098900 | biological_process | regulation of action potential |
A | 0098978 | cellular_component | glutamatergic synapse |
A | 1901379 | biological_process | regulation of potassium ion transmembrane transport |
A | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
A | 1990031 | cellular_component | pinceau fiber |
A | 2000008 | biological_process | regulation of protein localization to cell surface |
B | 0005216 | molecular_function | monoatomic ion channel activity |
B | 0005249 | molecular_function | voltage-gated potassium channel activity |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0006813 | biological_process | potassium ion transport |
B | 0008076 | cellular_component | voltage-gated potassium channel complex |
B | 0016020 | cellular_component | membrane |
B | 0051260 | biological_process | protein homooligomerization |
B | 0055085 | biological_process | transmembrane transport |
G | 0002244 | biological_process | hematopoietic progenitor cell differentiation |
G | 0004033 | molecular_function | aldo-keto reductase (NADPH) activity |
G | 0005249 | molecular_function | voltage-gated potassium channel activity |
G | 0005515 | molecular_function | protein binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0005829 | cellular_component | cytosol |
G | 0005856 | cellular_component | cytoskeleton |
G | 0005874 | cellular_component | microtubule |
G | 0005886 | cellular_component | plasma membrane |
G | 0006813 | biological_process | potassium ion transport |
G | 0008076 | cellular_component | voltage-gated potassium channel complex |
G | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
G | 0014069 | cellular_component | postsynaptic density |
G | 0015459 | molecular_function | potassium channel regulator activity |
G | 0016020 | cellular_component | membrane |
G | 0016491 | molecular_function | oxidoreductase activity |
G | 0030424 | cellular_component | axon |
G | 0034705 | cellular_component | potassium channel complex |
G | 0043005 | cellular_component | neuron projection |
G | 0043194 | cellular_component | axon initial segment |
G | 0043679 | cellular_component | axon terminus |
G | 0044224 | cellular_component | juxtaparanode region of axon |
G | 0044325 | molecular_function | transmembrane transporter binding |
G | 0044877 | molecular_function | protein-containing complex binding |
G | 0045202 | cellular_component | synapse |
G | 0045445 | biological_process | myoblast differentiation |
G | 0050905 | biological_process | neuromuscular process |
G | 0055085 | biological_process | transmembrane transport |
G | 0055114 | biological_process | obsolete oxidation-reduction process |
G | 0070995 | biological_process | NADPH oxidation |
G | 0071805 | biological_process | potassium ion transmembrane transport |
G | 0098839 | cellular_component | postsynaptic density membrane |
G | 0098900 | biological_process | regulation of action potential |
G | 0098978 | cellular_component | glutamatergic synapse |
G | 1901379 | biological_process | regulation of potassium ion transmembrane transport |
G | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
G | 1990031 | cellular_component | pinceau fiber |
G | 2000008 | biological_process | regulation of protein localization to cell surface |
H | 0005216 | molecular_function | monoatomic ion channel activity |
H | 0005249 | molecular_function | voltage-gated potassium channel activity |
H | 0006811 | biological_process | monoatomic ion transport |
H | 0006813 | biological_process | potassium ion transport |
H | 0008076 | cellular_component | voltage-gated potassium channel complex |
H | 0016020 | cellular_component | membrane |
H | 0051260 | biological_process | protein homooligomerization |
H | 0055085 | biological_process | transmembrane transport |
Y | 0005576 | cellular_component | extracellular region |
Y | 0008200 | molecular_function | ion channel inhibitor activity |
Y | 0015459 | molecular_function | potassium channel regulator activity |
Y | 0031640 | biological_process | killing of cells of another organism |
Y | 0035821 | biological_process | modulation of process of another organism |
Y | 0042742 | biological_process | defense response to bacterium |
Y | 0050832 | biological_process | defense response to fungus |
Y | 0090729 | molecular_function | toxin activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE NAP A 1001 |
Chain | Residue |
A | GLY55 |
A | ARG189 |
A | GLN214 |
A | TRP243 |
A | SER244 |
A | PRO245 |
A | LEU246 |
A | ALA247 |
A | CYS248 |
A | GLY249 |
A | LYS254 |
A | THR56 |
A | TYR262 |
A | SER263 |
A | ARG264 |
A | PRO304 |
A | LEU322 |
A | GLY323 |
A | SER325 |
A | GLN329 |
A | GLU332 |
A | ASN333 |
A | TRP57 |
A | HOH1140 |
A | HOH1141 |
A | HOH1167 |
A | HOH1230 |
A | GLN63 |
A | ASP85 |
A | TYR90 |
A | LYS118 |
A | ASN158 |
A | SER188 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE K B 501 |
Chain | Residue |
B | GLY372 |
B | GLY372 |
B | GLY372 |
B | GLY372 |
B | TYR373 |
B | TYR373 |
B | TYR373 |
B | TYR373 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE K B 502 |
Chain | Residue |
B | VAL371 |
B | VAL371 |
B | VAL371 |
B | VAL371 |
B | GLY372 |
B | GLY372 |
B | GLY372 |
B | GLY372 |
B | K503 |
B | K503 |
B | K503 |
B | K503 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE K B 503 |
Chain | Residue |
B | THR370 |
B | THR370 |
B | THR370 |
B | THR370 |
B | VAL371 |
B | VAL371 |
B | VAL371 |
B | VAL371 |
B | K502 |
B | K502 |
B | K502 |
B | K502 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K B 504 |
Chain | Residue |
B | THR370 |
B | THR370 |
B | THR370 |
B | THR370 |
site_id | AC6 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PGW B 505 |
Chain | Residue |
B | ILE328 |
B | PRO358 |
B | PHE361 |
B | ILE381 |
B | LYS384 |
B | SER388 |
B | PGW509 |
B | PGW510 |
site_id | AC7 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PGW B 506 |
Chain | Residue |
B | PGW507 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PGW B 507 |
Chain | Residue |
B | PGW506 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PGW B 509 |
Chain | Residue |
B | ILE385 |
B | PGW505 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PGW B 510 |
Chain | Residue |
B | VAL178 |
B | PGW505 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PGW B 511 |
Chain | Residue |
B | ILE328 |
B | THR397 |
B | PGW512 |
B | PGW516 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PGW B 512 |
Chain | Residue |
B | MET321 |
B | GLY325 |
B | PGW511 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PGW B 514 |
Chain | Residue |
B | PHE222 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PGW B 515 |
Chain | Residue |
B | SER307 |
B | LYS308 |
B | GLY309 |
B | ARG322 |
B | GLY325 |
B | LEU326 |
site_id | BC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PGW B 516 |
Chain | Residue |
B | PGW511 |
site_id | BC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PGW B 517 |
Chain | Residue |
B | LYS308 |
B | LEU310 |
B | GLN311 |
B | GLY314 |
B | ARG415 |
B | GLU416 |
B | PHE301 |
site_id | BC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PGW B 519 |
Chain | Residue |
B | ILE257 |
B | ILE264 |
site_id | BC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PGW B 520 |
Chain | Residue |
B | PHE218 |
site_id | CC1 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE NAP G 1001 |
Chain | Residue |
G | GLY55 |
G | THR56 |
G | TRP57 |
G | GLN63 |
G | ASP85 |
G | TYR90 |
G | LYS118 |
G | ASN158 |
G | SER188 |
G | ARG189 |
G | GLN214 |
G | TRP243 |
G | SER244 |
G | PRO245 |
G | LEU246 |
G | CYS248 |
G | GLY249 |
G | SER252 |
G | LYS254 |
G | TYR262 |
G | SER263 |
G | ARG264 |
G | PRO304 |
G | LEU322 |
G | GLY323 |
G | ALA324 |
G | SER325 |
G | GLN329 |
G | GLU332 |
G | ASN333 |
G | HOH1135 |
G | HOH1136 |
G | HOH1150 |
site_id | CC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE K H 501 |
Chain | Residue |
H | GLY372 |
H | GLY372 |
H | GLY372 |
H | GLY372 |
H | TYR373 |
H | TYR373 |
H | TYR373 |
H | TYR373 |
H | K502 |
H | K502 |
H | K502 |
H | K502 |
site_id | CC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE K H 502 |
Chain | Residue |
H | VAL371 |
H | VAL371 |
H | VAL371 |
H | VAL371 |
H | GLY372 |
H | GLY372 |
H | GLY372 |
H | GLY372 |
H | K501 |
H | K501 |
H | K501 |
H | K501 |
H | K503 |
H | K503 |
H | K503 |
H | K503 |
site_id | CC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE K H 503 |
Chain | Residue |
H | THR370 |
H | THR370 |
H | THR370 |
H | THR370 |
H | VAL371 |
H | VAL371 |
H | VAL371 |
H | VAL371 |
H | K502 |
H | K502 |
H | K502 |
H | K502 |
H | K504 |
H | K504 |
H | K504 |
H | K504 |
site_id | CC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE K H 504 |
Chain | Residue |
H | THR370 |
H | THR370 |
H | THR370 |
H | THR370 |
H | K503 |
H | K503 |
H | K503 |
H | K503 |
site_id | CC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PGW H 505 |
Chain | Residue |
H | PRO358 |
H | TRP362 |
H | VAL365 |
H | ILE381 |
H | LYS384 |
H | SER388 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Basic residue of the functional dyad => ECO:0000250 |
Chain | Residue | Details |
Y | MET27 | |
B | CYS244-ILE254 | |
B | SER307-MET321 | |
H | MET1-GLY160 | |
H | CYS244-ILE254 | |
H | SER307-MET321 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Aromatic residue of the functional dyad => ECO:0000250 |
Chain | Residue | Details |
Y | TYR36 | |
A | LYS254 | |
A | ARG264 | |
A | SER325 | |
A | GLN329 | |
A | ASN333 | |
G | THR56 | |
G | TRP57 | |
G | GLN63 | |
G | ASP85 | |
G | SER188 | |
H | PRO161-LEU182 | |
G | GLN214 | |
G | TRP243 | |
G | SER244 | |
G | LEU246 | |
G | LYS254 | |
G | ARG264 | |
G | SER325 | |
G | GLN329 | |
G | ASN333 | |
A | GLN63 | |
A | ASP85 | |
A | SER188 | |
A | GLN214 | |
A | TRP243 | |
A | SER244 | |
A | LEU246 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:2453055, ECO:0000269|PubMed:2482078 |
Chain | Residue | Details |
Y | PCA1 | |
H | GLU183-PRO221 |
site_id | SWS_FT_FI4 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=Segment S2 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
Chain | Residue | Details |
B | PHE222-ALA243 | |
H | PHE222-ALA243 |
site_id | SWS_FT_FI5 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=Segment S5 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
Chain | Residue | Details |
B | ARG322-TYR343 | |
H | ARG322-TYR343 |
site_id | SWS_FT_FI6 |
Number of Residues | 38 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
Chain | Residue | Details |
B | PHE344-ILE357 | |
B | PRO378-LYS384 | |
H | PHE344-ILE357 | |
H | PRO378-LYS384 |
site_id | SWS_FT_FI7 |
Number of Residues | 22 |
Details | INTRAMEM: Helical; Name=Pore helix => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
Chain | Residue | Details |
B | PRO358-THR369 | |
H | PRO358-THR369 |
site_id | SWS_FT_FI8 |
Number of Residues | 14 |
Details | INTRAMEM: INTRAMEM => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
Chain | Residue | Details |
B | THR370-VAL377 | |
H | THR370-VAL377 |
site_id | SWS_FT_FI9 |
Number of Residues | 56 |
Details | TRANSMEM: Helical; Name=Segment S6 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
Chain | Residue | Details |
B | ILE385-TYR413 | |
H | ILE385-TYR413 |
site_id | SWS_FT_FI10 |
Number of Residues | 162 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:12151401, ECO:0000305 |
Chain | Residue | Details |
B | HIS414-VAL495 | |
H | HIS414-VAL495 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | SITE: Important for normal, slow channel gating => ECO:0000269|PubMed:17766348 |
Chain | Residue | Details |
B | THR252 | |
H | THR252 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | SITE: Important for binding with the scorpion mesomartoxin; when the scorpion mesomartoxin-rKv1.2/KCNA2 interaction is modeled, this residue is close to the 'Y-57' residue of the toxin => ECO:0000305|PubMed:25514171 |
Chain | Residue | Details |
B | VAL377 | |
H | VAL377 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P63141 |
Chain | Residue | Details |
B | TYR425 | |
H | TYR425 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63141 |
Chain | Residue | Details |
B | SER430 | |
H | SER430 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18003609, ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
B | SER436 | |
H | SER436 |
site_id | SWS_FT_FI16 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
B | SER437 | |
B | SER464 | |
H | SER437 | |
H | SER464 |
site_id | SWS_FT_FI17 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18003609, ECO:0000269|PubMed:21602278 |
Chain | Residue | Details |
B | SER445 | |
H | SER445 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000305|PubMed:21602278 |
Chain | Residue | Details |
B | TYR454 | |
H | TYR454 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000255 |
Chain | Residue | Details |
B | CYS244 | |
H | CYS244 |
site_id | SWS_FT_FI20 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:16770729 |
Chain | Residue | Details |
B | GLN207 | |
H | GLN207 |
site_id | SWS_FT_FI21 |
Number of Residues | 26 |
Details | TOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P63142 |
Chain | Residue | Details |
B | GLU274-ARG287 | |
H | GLU274-ARG287 |