Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004089 | molecular_function | carbonate dehydratase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0008270 | molecular_function | zinc ion binding |
A | 0015670 | biological_process | carbon dioxide transport |
A | 0016020 | cellular_component | membrane |
A | 0016829 | molecular_function | lyase activity |
A | 0018820 | molecular_function | cyanamide hydratase activity |
A | 0038166 | biological_process | angiotensin-activated signaling pathway |
A | 0044070 | biological_process | regulation of monoatomic anion transport |
A | 0045177 | cellular_component | apical part of cell |
A | 0046872 | molecular_function | metal ion binding |
A | 0051453 | biological_process | regulation of intracellular pH |
A | 2001150 | biological_process | positive regulation of dipeptide transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue CU A 301 |
Chain | Residue |
A | HIS2 |
A | HIS9 |
A | HIS14 |
A | ASP18 |
A | HOH571 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue CU A 302 |
Chain | Residue |
A | ASP150 |
A | E68308 |
A | HOH538 |
A | HOH548 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue CU A 303 |
Chain | Residue |
A | HIS3 |
A | TRP4 |
A | HIS63 |
A | HOH401 |
A | HOH575 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue CU A 304 |
Chain | Residue |
A | HIS3 |
A | HIS63 |
A | HOH553 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ZN A 305 |
Chain | Residue |
A | HIS93 |
A | HIS95 |
A | HIS118 |
A | E68308 |
site_id | AC6 |
Number of Residues | 3 |
Details | binding site for residue GOL A 306 |
Chain | Residue |
A | TYR6 |
A | TRP243 |
A | HOH433 |
site_id | AC7 |
Number of Residues | 10 |
Details | binding site for residue GOL A 307 |
Chain | Residue |
A | ASN61 |
A | HIS63 |
A | SER64 |
A | ASN66 |
A | GLN91 |
A | HIS93 |
A | E68308 |
A | HOH424 |
A | HOH503 |
A | HOH506 |
site_id | AC8 |
Number of Residues | 18 |
Details | binding site for residue E68 A 308 |
Chain | Residue |
A | ASP71 |
A | VAL90 |
A | GLN91 |
A | HIS93 |
A | HIS95 |
A | HIS118 |
A | VAL120 |
A | PHE129 |
A | ASP150 |
A | LEU196 |
A | THR197 |
A | THR198 |
A | TRP207 |
A | CU302 |
A | ZN305 |
A | GOL307 |
A | HOH410 |
A | HOH549 |
Functional Information from PROSITE/UniProt
site_id | PS00162 |
Number of Residues | 17 |
Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdrkkYaaELHLV |
Chain | Residue | Details |
A | SER104-VAL120 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 256 |
Details | Domain: {"description":"Alpha-carbonic anhydrase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01134","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15039588","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Site: {"description":"Fine-tunes the proton-transfer properties of H-64","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P27139","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |