3LNM
F233W mutant of the Kv2.1 paddle-Kv1.2 chimera channel
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 |
C | 0002244 | biological_process | hematopoietic progenitor cell differentiation |
C | 0004033 | molecular_function | aldo-keto reductase (NADPH) activity |
C | 0005249 | molecular_function | voltage-gated potassium channel activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0005856 | cellular_component | cytoskeleton |
C | 0005874 | cellular_component | microtubule |
C | 0005886 | cellular_component | plasma membrane |
C | 0006813 | biological_process | potassium ion transport |
C | 0008076 | cellular_component | voltage-gated potassium channel complex |
C | 0009898 | cellular_component | cytoplasmic side of plasma membrane |
C | 0014069 | cellular_component | postsynaptic density |
C | 0015459 | molecular_function | potassium channel regulator activity |
C | 0016020 | cellular_component | membrane |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0030424 | cellular_component | axon |
C | 0034705 | cellular_component | potassium channel complex |
C | 0043005 | cellular_component | neuron projection |
C | 0043194 | cellular_component | axon initial segment |
C | 0043679 | cellular_component | axon terminus |
C | 0044224 | cellular_component | juxtaparanode region of axon |
C | 0044325 | molecular_function | transmembrane transporter binding |
C | 0044877 | molecular_function | protein-containing complex binding |
C | 0045202 | cellular_component | synapse |
C | 0045445 | biological_process | myoblast differentiation |
C | 0050905 | biological_process | neuromuscular process |
C | 0055085 | biological_process | transmembrane transport |
C | 0055114 | biological_process | obsolete oxidation-reduction process |
C | 0070995 | biological_process | NADPH oxidation |
C | 0071805 | biological_process | potassium ion transmembrane transport |
C | 0098839 | cellular_component | postsynaptic density membrane |
C | 0098900 | biological_process | regulation of action potential |
C | 0098978 | cellular_component | glutamatergic synapse |
C | 1901379 | biological_process | regulation of potassium ion transmembrane transport |
C | 1990002 | molecular_function | methylglyoxal reductase (NADPH) (acetol producing) activity |
C | 1990031 | cellular_component | pinceau fiber |
C | 2000008 | biological_process | regulation of protein localization to cell surface |
D | 0005216 | molecular_function | monoatomic ion channel activity |
D | 0005249 | molecular_function | voltage-gated potassium channel activity |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0006813 | biological_process | potassium ion transport |
D | 0008076 | cellular_component | voltage-gated potassium channel complex |
D | 0016020 | cellular_component | membrane |
D | 0051260 | biological_process | protein homooligomerization |
D | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 28 |
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 | SER263 |
A | ARG264 |
A | LEU321 |
A | GLY323 |
A | SER325 |
A | GLN329 |
A | GLU332 |
A | ASN333 |
A | HOH2036 |
A | TRP57 |
A | GLN63 |
A | ASP85 |
A | TYR90 |
A | LYS118 |
A | ASN158 |
A | SER188 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PGW B 601 |
Chain | Residue |
B | ILE328 |
B | PRO358 |
B | PHE361 |
B | TRP362 |
B | LYS384 |
B | SER388 |
B | PGW605 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PGW B 602 |
Chain | Residue |
B | HOH2130 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PGW B 605 |
Chain | Residue |
B | VAL178 |
B | PGW601 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PGW B 606 |
Chain | Residue |
B | THR397 |
B | PGW609 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PGW B 608 |
Chain | Residue |
B | SER307 |
B | LYS308 |
B | GLY309 |
B | ARG322 |
B | LEU326 |
B | PHE329 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PGW B 609 |
Chain | Residue |
B | PHE330 |
B | THR397 |
B | PGW606 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PGW B 610 |
Chain | Residue |
B | ILE254 |
B | MET255 |
B | LYS308 |
B | GLN311 |
B | GLY314 |
B | GLN315 |
B | LYS318 |
B | ARG415 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PGW B 611 |
Chain | Residue |
B | GLN214 |
B | SER215 |
B | THR216 |
B | ILE231 |
site_id | BC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE PGW B 612 |
Chain | Residue |
B | PHE218 |
site_id | BC2 |
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 | BC3 |
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 | BC4 |
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 | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE K B 504 |
Chain | Residue |
B | THR370 |
B | THR370 |
B | THR370 |
B | THR370 |
site_id | BC6 |
Number of Residues | 30 |
Details | BINDING SITE FOR RESIDUE NAP C 1001 |
Chain | Residue |
C | THR56 |
C | TRP57 |
C | GLN63 |
C | ASP85 |
C | TYR90 |
C | ASN158 |
C | SER188 |
C | ARG189 |
C | GLN214 |
C | TRP243 |
C | SER244 |
C | PRO245 |
C | LEU246 |
C | ALA247 |
C | CYS248 |
C | GLY249 |
C | SER252 |
C | LYS254 |
C | TYR262 |
C | SER263 |
C | ARG264 |
C | LEU321 |
C | GLY323 |
C | SER325 |
C | GLN329 |
C | GLU332 |
C | ASN333 |
C | HOH2028 |
C | HOH2038 |
C | GLY55 |
site_id | BC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PGW D 601 |
Chain | Residue |
D | PRO358 |
D | PHE361 |
D | TRP362 |
D | VAL365 |
D | ILE381 |
D | LYS384 |
D | SER388 |
site_id | BC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE K D 501 |
Chain | Residue |
D | GLY372 |
D | GLY372 |
D | GLY372 |
D | GLY372 |
D | TYR373 |
D | TYR373 |
D | TYR373 |
D | TYR373 |
D | K502 |
D | K502 |
D | K502 |
D | K502 |
site_id | BC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE K D 502 |
Chain | Residue |
D | VAL371 |
D | VAL371 |
D | VAL371 |
D | VAL371 |
D | GLY372 |
D | GLY372 |
D | GLY372 |
D | GLY372 |
D | K501 |
D | K501 |
D | K501 |
D | K501 |
site_id | CC1 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE K D 503 |
Chain | Residue |
D | THR370 |
D | THR370 |
D | THR370 |
D | THR370 |
D | VAL371 |
D | VAL371 |
D | VAL371 |
D | VAL371 |
D | K504 |
D | K504 |
D | K504 |
D | K504 |
site_id | CC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE K D 504 |
Chain | Residue |
D | THR370 |
D | THR370 |
D | THR370 |
D | THR370 |
D | K503 |
D | K503 |
D | K503 |
D | K503 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 366 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
Chain | Residue | Details |
B | MET1-GLY160 | |
B | CYS244-ILE254 | |
B | SER307-MET321 | |
D | MET1-GLY160 | |
D | CYS244-ILE254 | |
D | SER307-MET321 |
site_id | SWS_FT_FI2 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=Segment S1 => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430 |
Chain | Residue | Details |
B | PRO161-LEU182 | |
A | LYS254 | |
A | ARG264 | |
A | SER325 | |
A | GLN329 | |
A | ASN333 | |
C | THR56 | |
C | TRP57 | |
C | GLN63 | |
C | ASP85 | |
C | SER188 | |
D | PRO161-LEU182 | |
C | GLN214 | |
C | TRP243 | |
C | SER244 | |
C | LEU246 | |
C | LYS254 | |
C | ARG264 | |
C | SER325 | |
C | GLN329 | |
C | ASN333 | |
A | GLN63 | |
A | ASP85 | |
A | SER188 | |
A | GLN214 | |
A | TRP243 | |
A | SER244 | |
A | LEU246 |
site_id | SWS_FT_FI3 |
Number of Residues | 76 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430, ECO:0000305|PubMed:12151401 |
Chain | Residue | Details |
B | GLU183-PRO221 | |
D | 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 | |
D | 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 | |
D | 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 | |
D | PHE344-ILE357 | |
D | 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 | |
D | 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 | |
D | 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 | |
D | 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 | |
D | 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 | |
D | 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 | |
D | VAL377 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P63141 |
Chain | Residue | Details |
B | TYR425 | |
D | TYR425 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P63141 |
Chain | Residue | Details |
B | SER430 | |
D | 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 | |
D | 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 | |
D | SER437 | |
D | 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 | |
D | SER445 |
site_id | SWS_FT_FI18 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0000305|PubMed:21602278 |
Chain | Residue | Details |
B | TYR454 | |
D | TYR454 |
site_id | SWS_FT_FI19 |
Number of Residues | 2 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000255 |
Chain | Residue | Details |
B | CYS244 | |
D | 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 | |
D | GLN207 |
site_id | SWS_FT_FI21 |
Number of Residues | 26 |
Details | TOPO_DOM: Extracellular => ECO:0000250|UniProtKB:P63142 |
Chain | Residue | Details |
B | GLU274-ARG287 | |
D | GLU274-ARG287 |