1JV0
THE CRYSTAL STRUCTURE OF THE ZINC(II) ADDUCT OF THE CAI MICHIGAN 1 VARIANT
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 261 |
| Chain | Residue |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | EDO265 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 262 |
| Chain | Residue |
| A | HIS64 |
| A | ARG67 |
| A | HIS200 |
| A | CL263 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 263 |
| Chain | Residue |
| A | ARG67 |
| A | HIS200 |
| A | ZN262 |
| A | HOH290 |
| A | HIS64 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 264 |
| Chain | Residue |
| A | HIS243 |
| A | HOH351 |
| A | HOH380 |
| A | HOH418 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 261 |
| Chain | Residue |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | EDO265 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 262 |
| Chain | Residue |
| B | HIS64 |
| B | ARG67 |
| B | HIS200 |
| B | CL263 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 263 |
| Chain | Residue |
| B | HIS64 |
| B | ARG67 |
| B | HIS94 |
| B | HIS200 |
| B | ZN262 |
| B | HOH1384 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 264 |
| Chain | Residue |
| B | HIS243 |
| B | CL1266 |
| B | HOH1402 |
| B | HOH1467 |
| B | HOH1470 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL B 1266 |
| Chain | Residue |
| B | GLN242 |
| B | HIS243 |
| B | ZN264 |
| B | HOH1470 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 265 |
| Chain | Residue |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | LEU198 |
| A | THR199 |
| A | ZN261 |
| A | HOH290 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 265 |
| Chain | Residue |
| B | HIS94 |
| B | HIS96 |
| B | HIS119 |
| B | LEU198 |
| B | THR199 |
| B | ZN261 |
| B | HOH1384 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ca2 |
| Chain | Residue | Details |
| A | THR199 | |
| A | HIS64 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ca2 |
| Chain | Residue | Details |
| B | THR199 | |
| B | HIS64 |
