3OTQ
Soluble Epoxide Hydrolase in complex with pyrazole antagonist
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001558 | biological_process | regulation of cell growth |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004301 | molecular_function | epoxide hydrolase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005782 | cellular_component | peroxisomal matrix |
| 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 | 0070062 | cellular_component | extracellular exosome |
| A | 0090181 | biological_process | regulation of cholesterol metabolic process |
| A | 0097176 | biological_process | epoxide metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE MZL A 556 |
| Chain | Residue |
| A | PHE267 |
| A | LEU428 |
| A | TYR466 |
| A | VAL498 |
| A | HIS524 |
| A | TRP525 |
| A | ASP335 |
| A | TRP336 |
| A | MET339 |
| A | TYR383 |
| A | SER407 |
| A | LEU408 |
| A | ARG410 |
| A | MET419 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 |
| Chain | Residue | Details |
| A | ASP335 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 |
| Chain | Residue | Details |
| A | TYR466 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 |
| Chain | Residue | Details |
| A | HIS524 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15096040 |
| Chain | Residue | Details |
| A | ASP9 | |
| A | ASP11 | |
| A | THR123 | |
| A | ASP185 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563, ECO:0000269|PubMed:19746975, ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334 |
| Chain | Residue | Details |
| A | TYR383 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LYS43 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P34914 |
| Chain | Residue | Details |
| A | LYS55 | |
| A | LYS421 | |
| A | LYS455 | |
| A | LYS554 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P34914 |
| Chain | Residue | Details |
| A | LYS191 | |
| A | LYS215 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P34914 |
| Chain | Residue | Details |
| A | SER370 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | LIPID: S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine => ECO:0000305|PubMed:21164107 |
| Chain | Residue | Details |
| A | CYS522 |
