7Y1J
Structure of SUR2A in complex with Mg-ATP and repaglinide in the inward-facing conformation.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001669 | cellular_component | acrosomal vesicle |
| A | 0005267 | molecular_function | potassium channel activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006813 | biological_process | potassium ion transport |
| A | 0006932 | biological_process | substrate-dependent cell migration, cell contraction |
| A | 0008281 | molecular_function | sulfonylurea receptor activity |
| A | 0008282 | cellular_component | inward rectifying potassium channel |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0015459 | molecular_function | potassium channel regulator activity |
| A | 0016020 | cellular_component | membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0019829 | molecular_function | ATPase-coupled monoatomic cation transmembrane transporter activity |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0030315 | cellular_component | T-tubule |
| A | 0031004 | cellular_component | potassium ion-transporting ATPase complex |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0033198 | biological_process | response to ATP |
| A | 0042383 | cellular_component | sarcolemma |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0071805 | biological_process | potassium ion transmembrane transport |
| A | 0098655 | biological_process | monoatomic cation transmembrane transport |
| A | 0099104 | molecular_function | potassium channel activator activity |
| A | 0140359 | molecular_function | ABC-type transporter activity |
| A | 1901363 | molecular_function | heterocyclic compound binding |
| A | 1990573 | biological_process | potassium ion import across plasma membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00211 |
| Number of Residues | 15 |
| Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRQRICVARAL |
| Chain | Residue | Details |
| A | LEU808-LEU822 | |
| A | PHE1445-PHE1459 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 176 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=8","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 124 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=10","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=11","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=12","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=13","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=14","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=15","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 234 |
| Details | Domain: {"description":"ABC transporter 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
