4Y2P
Structure of soluble epoxide hydrolase in complex with N-methyl-1-[3-(pyridin-3-yl)phenyl]methanamine
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 | 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 | 4 |
Details | binding site for residue MG A 601 |
Chain | Residue |
A | ASP9 |
A | ASP11 |
A | ASP185 |
A | ILE186 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue 3C5 A 602 |
Chain | Residue |
A | PHE267 |
A | ASP335 |
A | TYR383 |
A | TYR466 |
A | HOH771 |
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 |