2GLQ
X-ray structure of human alkaline phosphatase in complex with strontium
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004035 | molecular_function | alkaline phosphatase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0009986 | cellular_component | cell surface |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0098552 | cellular_component | side of membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00123 |
| Number of Residues | 9 |
| Details | ALKALINE_PHOSPHATASE Alkaline phosphatase active site. VpDSGATAT |
| Chain | Residue | Details |
| A | VAL89-THR97 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Phosphoserine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10042","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11124260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15946677","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16815919","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20693656","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P05186","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15946677","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16815919","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20693656","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1alk |
| Chain | Residue | Details |
| A | ARG166 |
