5AM4
ligand complex structure of 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 | 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 | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1548 |
Chain | Residue |
A | GLN42 |
A | LYS43 |
A | GLY44 |
A | ARG194 |
A | HOH2075 |
A | HOH2315 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1549 |
Chain | Residue |
A | GLN384 |
A | LEU499 |
A | ASP335 |
A | TRP336 |
A | MET339 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS A 1550 |
Chain | Residue |
A | SER407 |
A | ARG410 |
A | SER415 |
A | LEU417 |
A | ASN431 |
A | PRO436 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMS A 1551 |
Chain | Residue |
A | LEU228 |
A | ARG440 |
A | MET441 |
A | VAL442 |
A | THR443 |
A | HOH2420 |
A | HOH2671 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS A 1552 |
Chain | Residue |
A | GLN283 |
A | GLY325 |
A | HOH2421 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS A 1553 |
Chain | Residue |
A | LYS144 |
A | PHE147 |
A | PHE149 |
A | HOH2237 |
A | HOH2457 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 1554 |
Chain | Residue |
A | ARG34 |
A | GLY35 |
A | THR200 |
A | HOH2060 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE MVJ A 1555 |
Chain | Residue |
A | TYR383 |
A | PHE387 |
A | LEU408 |
A | VAL416 |
A | LEU417 |
A | MET419 |
A | ASP496 |
A | PHE497 |
A | VAL498 |
A | HIS524 |
A | HOH2529 |
A | HOH2616 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMS A 1556 |
Chain | Residue |
A | ALA131 |
A | ARG133 |
A | ARG353 |
A | PRO487 |
A | ASP545 |
A | ARG547 |
A | HOH2466 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS A 1557 |
Chain | Residue |
A | ARG103 |
A | GLN107 |
A | LEU110 |
A | HIS146 |
A | THR230 |
A | HOH2194 |
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 | 3 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P34914 |
Chain | Residue | Details |
A | LYS55 | |
A | LYS421 | |
A | LYS455 |
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 |