6S2J
Square conformation of KtrA R16K mutant ring with bound ATP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005267 | molecular_function | potassium channel activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0006813 | biological_process | potassium ion transport |
| A | 0008324 | molecular_function | monoatomic cation transmembrane transporter activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0071805 | biological_process | potassium ion transmembrane transport |
| B | 0005267 | molecular_function | potassium channel activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0006813 | biological_process | potassium ion transport |
| B | 0008324 | molecular_function | monoatomic cation transmembrane transporter activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0071805 | biological_process | potassium ion transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue ATP A 601 |
| Chain | Residue |
| A | GLY13 |
| A | ASN56 |
| A | ALA57 |
| A | ILE78 |
| A | GLY79 |
| A | ALA80 |
| A | LYS103 |
| A | GLN105 |
| A | GLU125 |
| A | MG603 |
| A | HOH701 |
| A | LEU14 |
| A | HOH702 |
| B | GLU125 |
| A | GLY15 |
| A | LYS16 |
| A | PHE17 |
| A | ASP36 |
| A | ILE37 |
| A | LYS41 |
| A | ALA55 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue ATP A 602 |
| Chain | Residue |
| A | GLU125 |
| A | MG603 |
| A | HOH702 |
| B | GLY13 |
| B | LEU14 |
| B | GLY15 |
| B | LYS16 |
| B | PHE17 |
| B | ASP36 |
| B | ILE37 |
| B | LYS41 |
| B | ALA55 |
| B | ASN56 |
| B | ALA57 |
| B | ALA77 |
| B | GLY79 |
| B | ALA80 |
| B | LYS103 |
| B | GLN105 |
| B | GLU125 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 603 |
| Chain | Residue |
| A | GLU125 |
| A | ATP601 |
| A | ATP602 |
| A | HOH701 |
| A | HOH702 |
| B | GLU125 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 232 |
| Details | Domain: {"description":"RCK N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00543","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 166 |
| Details | Domain: {"description":"RCK C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00544","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12086676","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16990138","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
