5E2M
Crystal structure of human carbonic anhydrase isozyme I with 3-(cyclooctylamino)-2,5,6-trifluoro-4-[(2-hydroxyethyl)sulfonyl]benzenesulfonamide
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 | V14302 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue V14 A 302 |
| Chain | Residue |
| A | HIS119 |
| A | LEU131 |
| A | ALA135 |
| A | LEU198 |
| A | THR199 |
| A | HIS200 |
| A | PRO201 |
| A | PRO202 |
| A | TRP209 |
| A | ZN301 |
| A | ACT303 |
| A | HOH489 |
| A | HOH518 |
| B | ALA132 |
| A | HIS64 |
| A | HIS67 |
| A | PHE91 |
| A | HIS94 |
| A | HIS96 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 303 |
| Chain | Residue |
| A | TYR204 |
| A | V14302 |
| A | HOH402 |
| B | TYR204 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 301 |
| Chain | Residue |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | V14302 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue V14 B 302 |
| Chain | Residue |
| B | HIS64 |
| B | HIS67 |
| B | GLN92 |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | ALA135 |
| B | LEU198 |
| B | THR199 |
| B | HIS200 |
| B | PRO201 |
| B | PRO202 |
| B | ZN301 |
| B | HOH591 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue PEG B 303 |
| Chain | Residue |
| A | LYS172 |
| A | HOH413 |
| A | HOH415 |
| B | ASN52 |
| B | PRO53 |
| B | ALA54 |
| B | ASN178 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue PEG B 304 |
| Chain | Residue |
| B | ASP74 |
| B | ASN75 |
| B | ARG76 |
| B | ALA153 |
| B | PRO155 |
| B | GLN158 |
| B | HOH506 |
| B | HOH602 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide ASP B 72 and ARG B 89 |
| Chain | Residue |
| B | PHE70 |
| B | GLU71 |
| B | ASN73 |
| B | ASP74 |
| B | ASN75 |
| B | SER77 |
| B | TYR88 |
| B | LEU90 |
| B | PHE91 |
| B | HIS122 |
| B | TRP123 |
| B | HOH401 |
| B | HOH430 |
| B | HOH567 |
| B | HOH569 |
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 |
