2HFW
Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003009 | biological_process | skeletal muscle contraction |
A | 0004089 | molecular_function | carbonate dehydratase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006979 | biological_process | response to oxidative stress |
A | 0008270 | molecular_function | zinc ion binding |
A | 0008284 | biological_process | positive regulation of cell population proliferation |
A | 0009617 | biological_process | response to bacterium |
A | 0016151 | molecular_function | nickel cation binding |
A | 0016791 | molecular_function | phosphatase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0030017 | cellular_component | sarcomere |
A | 0032869 | biological_process | cellular response to insulin stimulus |
A | 0033993 | biological_process | response to lipid |
A | 0043066 | biological_process | negative regulation of apoptotic process |
A | 0044320 | biological_process | cellular response to leptin stimulus |
A | 0045471 | biological_process | response to ethanol |
A | 0046872 | molecular_function | metal ion binding |
A | 0071456 | biological_process | cellular response to hypoxia |
A | 0097305 | biological_process | response to alcohol |
A | 0097421 | biological_process | liver regeneration |
A | 1903427 | biological_process | negative regulation of reactive oxygen species biosynthetic process |
A | 1903751 | biological_process | negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 262 |
Chain | Residue |
A | HIS94 |
A | HIS96 |
A | HIS119 |
A | HOH326 |
Functional Information from PROSITE/UniProt
site_id | PS00162 |
Number of Residues | 17 |
Details | ALPHA_CA_1 Alpha-carbonic anhydrases signature. SEHtVdgvkYaaELHLV |
Chain | Residue | Details |
A | SER105-VAL121 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | Region: {"description":"Involved in proton transfer","evidences":[{"source":"PubMed","id":"17427958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"16042381","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17427958","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00918","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14141","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P14141","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14141","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P16015","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Modified residue: {"description":"S-glutathionyl cysteine","evidences":[{"source":"UniProtKB","id":"P14141","evidenceCode":"ECO:0000250"}]} |
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 |