1CRM
STRUCTURE AND FUNCTION OF CARBONIC ANHYDRASES
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 | 0006730 | biological_process | one-carbon metabolic process |
| A | 0008270 | molecular_function | zinc ion binding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE HG A 261 |
| Chain | Residue |
| A | HIS94 |
| A | HIS96 |
| A | HIS119 |
| A | THR199 |
| A | CL263 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE HG A 262 |
| Chain | Residue |
| A | CYS212 |
| A | HG264 |
| A | CL265 |
| A | H2S266 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 263 |
| Chain | Residue |
| A | THR199 |
| A | HG261 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE HG A 264 |
| Chain | Residue |
| A | SER188 |
| A | ASP190 |
| A | CYS212 |
| A | HG262 |
| A | CL265 |
| A | H2S266 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 265 |
| Chain | Residue |
| A | ILE47 |
| A | LEU189 |
| A | HG262 |
| A | HG264 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE HG A 267 |
| Chain | Residue |
| A | SER99 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE H2S A 266 |
| Chain | Residue |
| A | PRO186 |
| A | SER188 |
| A | CYS212 |
| A | LYS213 |
| A | HG262 |
| A | HG264 |
| site_id | CAT |
| Number of Residues | 24 |
| Details | RESIDUES TYR 7, VAL 62, HIS 64, SER 65, HIS 67, ASN 69, GLN 92, GLU 106, GLU 117, THR 199, HIS 200 ARE HYDROPHILIC, WHILE PHE 91, ALA 121, LEU 131, ALA 135, LEU 141, VAL 143, LEU 198, PRO 201, PRO 202, TYR 204, SER 206, VAL 207, TRP 209 ARE HYDROPHOBIC |
| Chain | Residue |
| A | TYR7 |
| A | GLU117 |
| A | ALA121 |
| A | LEU131 |
| A | ALA135 |
| A | LEU141 |
| A | VAL143 |
| A | LEU198 |
| A | THR199 |
| A | HIS200 |
| A | PRO201 |
| A | VAL62 |
| A | PRO202 |
| A | TYR204 |
| A | SER206 |
| A | VAL207 |
| A | TRP209 |
| A | HIS64 |
| A | SER65 |
| A | HIS67 |
| A | ASN69 |
| A | PHE91 |
| A | GLN92 |
| A | GLU106 |
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 | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P00918 |
| Chain | Residue | Details |
| A | SER65 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | BINDING: in variant Michigan-1 => ECO:0000269|PubMed:12009884 |
| Chain | Residue | Details |
| A | SER65 | |
| A | VAL68 | |
| A | PRO201 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12009884, ECO:0000269|PubMed:15299369, ECO:0000269|PubMed:16506782, ECO:0000269|PubMed:16870440, ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17407288, ECO:0000269|PubMed:6430186, ECO:0000269|PubMed:7932756, ECO:0000269|PubMed:804171, ECO:0000269|PubMed:8057362 |
| Chain | Residue | Details |
| A | PHE95 | |
| A | TRP97 | |
| A | VAL120 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:8057362 |
| Chain | Residue | Details |
| A | HIS200 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:4207120, ECO:0000269|PubMed:4217196 |
| Chain | Residue | Details |
| A | SER2 |
