6UQF
Human HCN1 channel in a hyperpolarized conformation
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0005249 | molecular_function | voltage-gated potassium channel activity |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0006813 | biological_process | potassium ion transport |
A | 0016020 | cellular_component | membrane |
A | 0055085 | biological_process | transmembrane transport |
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 | 0016020 | cellular_component | membrane |
B | 0055085 | biological_process | transmembrane transport |
C | 0005216 | molecular_function | monoatomic ion channel activity |
C | 0005249 | molecular_function | voltage-gated potassium channel activity |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0006813 | biological_process | potassium ion transport |
C | 0016020 | cellular_component | membrane |
C | 0055085 | biological_process | transmembrane transport |
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 | 0016020 | cellular_component | membrane |
D | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue CMP A 901 |
Chain | Residue |
A | MET530 |
A | ALA551 |
A | ARG590 |
A | ARG593 |
A | ILE594 |
A | LEU532 |
A | PHE538 |
A | GLY539 |
A | GLU540 |
A | ILE541 |
A | CYS542 |
A | ARG549 |
A | THR550 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue HG A 902 |
Chain | Residue |
A | CYS186 |
A | CYS264 |
site_id | AC3 |
Number of Residues | 13 |
Details | binding site for residue CMP B 901 |
Chain | Residue |
B | MET530 |
B | LEU532 |
B | PHE538 |
B | GLY539 |
B | GLU540 |
B | ILE541 |
B | CYS542 |
B | ARG549 |
B | THR550 |
B | ALA551 |
B | ARG590 |
B | ARG593 |
B | ILE594 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue HG B 902 |
Chain | Residue |
B | CYS186 |
B | CYS264 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue CMP C 901 |
Chain | Residue |
C | MET530 |
C | LEU532 |
C | PHE538 |
C | GLY539 |
C | GLU540 |
C | ILE541 |
C | CYS542 |
C | ARG549 |
C | THR550 |
C | ALA551 |
C | ARG590 |
C | ARG593 |
C | ILE594 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue HG C 902 |
Chain | Residue |
C | CYS186 |
C | CYS264 |
site_id | AC7 |
Number of Residues | 13 |
Details | binding site for residue CMP D 901 |
Chain | Residue |
D | MET530 |
D | LEU532 |
D | PHE538 |
D | GLY539 |
D | GLU540 |
D | ILE541 |
D | CYS542 |
D | ARG549 |
D | THR550 |
D | ALA551 |
D | ARG590 |
D | ARG593 |
D | ILE594 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue HG D 902 |
Chain | Residue |
D | CYS186 |
D | CYS264 |
Functional Information from PROSITE/UniProt
site_id | PS00888 |
Number of Residues | 17 |
Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. IIrEGAvGKkMYFIqhG |
Chain | Residue | Details |
A | ILE502-GLY518 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2684 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28086084 |
Chain | Residue | Details |
A | MET1-ARG142 | |
C | ARG195-MET215 | |
C | GLU282-VAL295 | |
D | MET1-ARG142 | |
D | ARG195-MET215 | |
D | GLU282-VAL295 | |
A | ARG195-MET215 | |
A | GLU282-VAL295 | |
B | MET1-ARG142 | |
B | ARG195-MET215 | |
B | GLU282-VAL295 | |
C | MET1-ARG142 |
site_id | SWS_FT_FI2 |
Number of Residues | 84 |
Details | TRANSMEM: Helical; Name=Segment S1 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG |
Chain | Residue | Details |
A | PHE143-ILE164 | |
B | PHE143-ILE164 | |
C | PHE143-ILE164 | |
D | PHE143-ILE164 |
site_id | SWS_FT_FI3 |
Number of Residues | 240 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:28086084 |
Chain | Residue | Details |
A | THR165-THR173 | |
C | LEU237-THR260 | |
C | VAL319-GLN344 | |
C | VAL367-ASP371 | |
D | THR165-THR173 | |
D | LEU237-THR260 | |
D | VAL319-GLN344 | |
D | VAL367-ASP371 | |
A | LEU237-THR260 | |
A | VAL319-GLN344 | |
A | VAL367-ASP371 | |
B | THR165-THR173 | |
B | LEU237-THR260 | |
B | VAL319-GLN344 | |
B | VAL367-ASP371 | |
C | THR165-THR173 |
site_id | SWS_FT_FI4 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=Segment S2 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG |
Chain | Residue | Details |
A | PRO174-PHE194 | |
B | PRO174-PHE194 | |
C | PRO174-PHE194 | |
D | PRO174-PHE194 |
site_id | SWS_FT_FI5 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=Segment S3 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG |
Chain | Residue | Details |
A | ASN216-PHE236 | |
B | ASN216-PHE236 | |
C | ASN216-PHE236 | |
D | ASN216-PHE236 |
site_id | SWS_FT_FI6 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Voltage-sensor; Name=Segment S4 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG |
Chain | Residue | Details |
A | LYS261-TRP281 | |
B | LYS261-TRP281 | |
C | LYS261-TRP281 | |
D | LYS261-TRP281 |
site_id | SWS_FT_FI7 |
Number of Residues | 88 |
Details | TRANSMEM: Helical; Name=Segment S5 => ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG |
Chain | Residue | Details |
A | VAL296-LEU318 | |
B | VAL296-LEU318 | |
C | VAL296-LEU318 | |
D | VAL296-LEU318 |
site_id | SWS_FT_FI8 |
Number of Residues | 84 |
Details | INTRAMEM: Pore-forming; Name=Segment H5 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG |
Chain | Residue | Details |
A | TYR345-PRO366 | |
B | TYR345-PRO366 | |
C | TYR345-PRO366 | |
D | TYR345-PRO366 |
site_id | SWS_FT_FI9 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=Segment S6 => ECO:0000269|PubMed:28086084, ECO:0000269|PubMed:31787376, ECO:0007744|PDB:5U6O, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF, ECO:0007744|PDB:6UQG |
Chain | Residue | Details |
A | LEU372-HIS392 | |
B | LEU372-HIS392 | |
C | LEU372-HIS392 | |
D | LEU372-HIS392 |
site_id | SWS_FT_FI10 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31787376, ECO:0000305|PubMed:28086084, ECO:0007744|PDB:5U6P, ECO:0007744|PDB:6UQF |
Chain | Residue | Details |
A | GLY539 | |
C | CYS542 | |
C | ARG549 | |
C | THR550 | |
D | GLY539 | |
D | CYS542 | |
D | ARG549 | |
D | THR550 | |
A | CYS542 | |
A | ARG549 | |
A | THR550 | |
B | GLY539 | |
B | CYS542 | |
B | ARG549 | |
B | THR550 | |
C | GLY539 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:31787376, ECO:0007744|PDB:6UQF |
Chain | Residue | Details |
A | GLU540 | |
A | ARG593 | |
B | GLU540 | |
B | ARG593 | |
C | GLU540 | |
C | ARG593 | |
D | GLU540 | |
D | ARG593 |
site_id | SWS_FT_FI12 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:O88704 |
Chain | Residue | Details |
A | ARG590 | |
B | ARG590 | |
C | ARG590 | |
D | ARG590 |
site_id | SWS_FT_FI13 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN338 | |
B | ASN338 | |
C | ASN338 | |
D | ASN338 |