4F8H
X-ray Structure of the Anesthetic Ketamine Bound to the GLIC Pentameric Ligand-gated Ion Channel
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004888 | molecular_function | transmembrane signaling receptor activity |
| A | 0005216 | molecular_function | monoatomic ion channel activity |
| A | 0005230 | molecular_function | extracellular ligand-gated monoatomic ion channel activity |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0016020 | cellular_component | membrane |
| A | 0034220 | biological_process | monoatomic ion transmembrane transport |
| B | 0004888 | molecular_function | transmembrane signaling receptor activity |
| B | 0005216 | molecular_function | monoatomic ion channel activity |
| B | 0005230 | molecular_function | extracellular ligand-gated monoatomic ion channel activity |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0016020 | cellular_component | membrane |
| B | 0034220 | biological_process | monoatomic ion transmembrane transport |
| C | 0004888 | molecular_function | transmembrane signaling receptor activity |
| C | 0005216 | molecular_function | monoatomic ion channel activity |
| C | 0005230 | molecular_function | extracellular ligand-gated monoatomic ion channel activity |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0016020 | cellular_component | membrane |
| C | 0034220 | biological_process | monoatomic ion transmembrane transport |
| D | 0004888 | molecular_function | transmembrane signaling receptor activity |
| D | 0005216 | molecular_function | monoatomic ion channel activity |
| D | 0005230 | molecular_function | extracellular ligand-gated monoatomic ion channel activity |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0016020 | cellular_component | membrane |
| D | 0034220 | biological_process | monoatomic ion transmembrane transport |
| E | 0004888 | molecular_function | transmembrane signaling receptor activity |
| E | 0005216 | molecular_function | monoatomic ion channel activity |
| E | 0005230 | molecular_function | extracellular ligand-gated monoatomic ion channel activity |
| E | 0006811 | biological_process | monoatomic ion transport |
| E | 0016020 | cellular_component | membrane |
| E | 0034220 | biological_process | monoatomic ion transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE RKE A 401 |
| Chain | Residue |
| A | TYR23 |
| A | ASN152 |
| A | ASP153 |
| A | ASP154 |
| B | PHE174 |
| B | LEU176 |
| B | LYS183 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE LMD A 402 |
| Chain | Residue |
| A | ILE233 |
| A | ALA237 |
| A | ILE240 |
| A | THR244 |
| A | ASN245 |
| B | THR244 |
| B | LMD402 |
| C | LMD405 |
| E | ILE233 |
| E | ALA234 |
| E | ALA237 |
| E | LMD402 |
| A | ASP31 |
| A | LYS33 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PC1 A 403 |
| Chain | Residue |
| A | PHE121 |
| A | TYR194 |
| A | TYR254 |
| A | ASN307 |
| A | PHE315 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PC1 A 404 |
| Chain | Residue |
| A | ARG118 |
| A | MET252 |
| A | MET261 |
| A | LEU313 |
| A | PHE314 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE RKE B 401 |
| Chain | Residue |
| B | TYR23 |
| B | ASN152 |
| B | ASP153 |
| B | ASP154 |
| C | VAL79 |
| C | PHE174 |
| C | LEU176 |
| C | LYS183 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE LMD B 402 |
| Chain | Residue |
| A | ALA234 |
| A | ALA237 |
| A | LMD402 |
| B | ASP31 |
| B | LYS33 |
| B | ILE233 |
| B | ALA237 |
| B | LEU241 |
| B | THR244 |
| B | ASN245 |
| B | HOH507 |
| C | LYS33 |
| C | THR244 |
| C | LMD402 |
| C | LMD405 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PC1 B 403 |
| Chain | Residue |
| B | ARG118 |
| B | PHE121 |
| B | TYR194 |
| B | TYR254 |
| B | ASN307 |
| B | PHE315 |
| B | PC1404 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PC1 B 404 |
| Chain | Residue |
| B | ARG118 |
| B | LEU313 |
| B | PC1403 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE RKE C 401 |
| Chain | Residue |
| C | TYR23 |
| C | ASN152 |
| C | ASP153 |
| C | ASP154 |
| D | VAL79 |
| D | PHE174 |
| D | LEU176 |
| D | LYS183 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE LMD C 402 |
| Chain | Residue |
| B | ILE233 |
| B | ALA234 |
| B | ALA237 |
| B | LMD402 |
| C | ASP31 |
| C | ILE233 |
| C | THR244 |
| C | ASN245 |
| C | LMD405 |
| D | LYS33 |
| D | LMD402 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PC1 C 403 |
| Chain | Residue |
| C | ARG118 |
| C | PHE121 |
| C | TYR194 |
| C | ILE198 |
| C | LEU206 |
| C | TYR254 |
| C | ASN307 |
| C | PHE315 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PC1 C 404 |
| Chain | Residue |
| B | PHE195 |
| C | TYR251 |
| C | MET252 |
| C | MET261 |
| C | LEU264 |
| site_id | BC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LMD C 405 |
| Chain | Residue |
| B | LMD402 |
| C | SER230 |
| C | ILE233 |
| C | LMD402 |
| D | ILE233 |
| D | LMD402 |
| E | SER230 |
| E | ILE233 |
| E | LMD402 |
| A | ILE233 |
| A | LMD402 |
| B | ILE233 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE RKE D 401 |
| Chain | Residue |
| D | TYR23 |
| D | ASN152 |
| D | ASP153 |
| D | ASP154 |
| E | PHE174 |
| E | LEU176 |
| E | LYS183 |
| site_id | BC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE LMD D 402 |
| Chain | Residue |
| C | ALA234 |
| C | ALA237 |
| C | LMD402 |
| C | LMD405 |
| D | ASP31 |
| D | ILE236 |
| D | ALA237 |
| D | ILE240 |
| D | THR244 |
| D | ASN245 |
| E | LYS33 |
| E | THR244 |
| E | LMD402 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PC1 D 403 |
| Chain | Residue |
| D | ARG118 |
| D | TYR194 |
| D | ILE198 |
| D | TYR254 |
| D | ASN307 |
| D | PHE315 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PC1 D 404 |
| Chain | Residue |
| C | PHE195 |
| D | ARG118 |
| D | MET252 |
| D | PHE260 |
| D | LEU313 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE RKE E 401 |
| Chain | Residue |
| A | VAL79 |
| A | PHE174 |
| A | LEU176 |
| A | LYS183 |
| E | TYR23 |
| E | ASN152 |
| E | ASP153 |
| E | ASP154 |
| site_id | CC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE LMD E 402 |
| Chain | Residue |
| A | LYS33 |
| A | THR244 |
| A | LMD402 |
| C | LMD405 |
| D | ILE233 |
| D | LMD402 |
| E | ASP31 |
| E | ILE233 |
| E | ALA237 |
| E | ILE240 |
| E | THR244 |
| E | ASN245 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PC1 E 403 |
| Chain | Residue |
| E | PHE121 |
| E | GLU163 |
| E | SER191 |
| E | TYR194 |
| E | TYR254 |
| E | ASN307 |
| E | PHE315 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PC1 E 404 |
| Chain | Residue |
| E | ARG118 |
| E | TYR251 |
| E | MET252 |
| E | LEU313 |
| E | PHE314 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 370 |
| Details | Transmembrane: {"description":"Helical"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 35 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






