6I0J
Crystal structure of human carbonic anhydrase I in complex with the 4-({[4-chloro-3-(trifluoromethyl)phenyl]carbamoyl}amino)phenyl sulfamate inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004064 | molecular_function | arylesterase activity |
| A | 0004089 | molecular_function | carbonate dehydratase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009750 | biological_process | response to fructose |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016836 | molecular_function | hydro-lyase activity |
| A | 0018820 | molecular_function | cyanamide hydratase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070062 | cellular_component | extracellular exosome |
| B | 0004064 | molecular_function | arylesterase activity |
| B | 0004089 | molecular_function | carbonate dehydratase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0009750 | biological_process | response to fructose |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016836 | molecular_function | hydro-lyase activity |
| B | 0018820 | molecular_function | cyanamide hydratase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 301 |
| Chain | Residue |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | GZE306 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue ACT A 302 |
| Chain | Residue |
| B | GZE303 |
| B | HOH421 |
| A | PRO202 |
| A | TYR204 |
| A | GZE306 |
| B | ALA132 |
| B | TYR204 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 303 |
| Chain | Residue |
| A | HIS103 |
| A | GLY104 |
| A | SER105 |
| A | ASN245 |
| A | HOH427 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | ALA138 |
| A | ASP139 |
| A | HOH485 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 305 |
| Chain | Residue |
| A | THR35 |
| A | PHE260 |
| A | HOH425 |
| A | HOH433 |
| B | HOH430 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue GZE A 306 |
| Chain | Residue |
| A | HIS67 |
| A | PHE91 |
| A | GLN92 |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | LEU131 |
| A | ALA135 |
| A | LEU141 |
| A | LEU198 |
| A | THR199 |
| A | HIS200 |
| A | PRO202 |
| A | TYR204 |
| A | TRP209 |
| A | ZN301 |
| A | ACT302 |
| A | HOH447 |
| B | GLU133 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | GZE303 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 302 |
| Chain | Residue |
| B | LYS149 |
| B | SER215 |
| B | ILE216 |
| B | SER217 |
| B | HOH547 |
| B | HOH587 |
| B | HOH618 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | binding site for residue GZE B 303 |
| Chain | Residue |
| A | ALA132 |
| A | TYR204 |
| A | ACT302 |
| B | HIS67 |
| B | GLN92 |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | LEU131 |
| B | ALA135 |
| B | LEU198 |
| B | THR199 |
| B | HIS200 |
| B | PRO202 |
| B | TYR204 |
| B | TRP209 |
| B | ZN301 |
| B | HOH598 |
Functional Information from PROSITE/UniProt
| site_id | PS00162 |
| Number of Residues | 17 |
| Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgvkYsaELHVA |
| Chain | Residue | Details |
| A | SER105-ALA121 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 40 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"description":"in variant Michigan-1","evidences":[{"source":"PubMed","id":"12009884","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12009884","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15299369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16506782","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16870440","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17314045","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17407288","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6430186","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7932756","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"804171","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8057362","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8057362","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
