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 | 0009056 | biological_process | catabolic 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 | 0009056 | biological_process | catabolic 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 | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:10485878, ECO:0000269|PubMed:10747889 |
Chain | Residue | Details |
A | ASP333 | |
B | ASP333 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:10485878, ECO:0000269|PubMed:10747889 |
Chain | Residue | Details |
A | TYR465 | |
B | TYR465 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:10485878, ECO:0000269|PubMed:10747889 |
Chain | Residue | Details |
A | HIS523 | |
B | HIS523 |
site_id | SWS_FT_FI4 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P34913 |
Chain | Residue | Details |
A | ASP9 | |
B | TYR381 | |
A | ASP11 | |
A | THR123 | |
A | ASP185 | |
A | TYR381 | |
B | ASP9 | |
B | ASP11 | |
B | THR123 | |
B | ASP185 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS55 | |
B | LYS454 | |
B | LYS504 | |
B | LYS553 | |
A | LYS371 | |
A | LYS420 | |
A | LYS454 | |
A | LYS504 | |
A | LYS553 | |
B | LYS55 | |
B | LYS371 | |
B | LYS420 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS176 | |
A | LYS508 | |
B | LYS176 | |
B | LYS508 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23576753 |
Chain | Residue | Details |
A | LYS191 | |
A | LYS215 | |
B | LYS191 | |
B | LYS215 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079 |
Chain | Residue | Details |
A | SER368 | |
B | SER368 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | LIPID: S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine => ECO:0000250 |
Chain | Residue | Details |
A | CYS521 | |
B | CYS521 |
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 |