1CQZ
CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004301 | molecular_function | epoxide hydrolase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0010628 | biological_process | positive regulation of gene expression |
| A | 0015643 | molecular_function | toxic substance binding |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0033885 | molecular_function | 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity |
| A | 0042577 | molecular_function | lipid phosphatase activity |
| A | 0042632 | biological_process | cholesterol homeostasis |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046272 | biological_process | stilbene catabolic process |
| A | 0046839 | biological_process | phospholipid dephosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0052642 | molecular_function | lysophosphatidic acid phosphatase activity |
| A | 0090181 | biological_process | regulation of cholesterol metabolic process |
| A | 0097176 | biological_process | epoxide metabolic process |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004301 | molecular_function | epoxide hydrolase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005777 | cellular_component | peroxisome |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0009636 | biological_process | response to toxic substance |
| B | 0010628 | biological_process | positive regulation of gene expression |
| B | 0015643 | molecular_function | toxic substance binding |
| B | 0016311 | biological_process | dephosphorylation |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016791 | molecular_function | phosphatase activity |
| B | 0033885 | molecular_function | 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity |
| B | 0042577 | molecular_function | lipid phosphatase activity |
| B | 0042632 | biological_process | cholesterol homeostasis |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046272 | biological_process | stilbene catabolic process |
| B | 0046839 | biological_process | phospholipid dephosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0052642 | molecular_function | lysophosphatidic acid phosphatase activity |
| B | 0090181 | biological_process | regulation of cholesterol metabolic process |
| B | 0097176 | biological_process | epoxide metabolic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 546 |
| Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"10485878","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10747889","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"10485878","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10747889","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10485878","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10747889","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P34913","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23576753","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17242355","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Lipidation: {"description":"S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b6g |
| Chain | Residue | Details |
| A | HIS523 | |
| A | ASP495 | |
| A | ASP333 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1b6g |
| Chain | Residue | Details |
| B | HIS523 | |
| B | ASP495 | |
| B | ASP333 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b6g |
| Chain | Residue | Details |
| A | THR123 | |
| A | LYS160 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1b6g |
| Chain | Residue | Details |
| B | THR123 | |
| B | LYS160 |
