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 | 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 | 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 | 272 |
| Details | Domain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16322563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19746975","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19969453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20934334","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16322563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19746975","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19969453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20934334","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16322563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19746975","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19969453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20934334","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16322563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19746975","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19969453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20934334","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P34914","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P34914","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P34914","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine","evidences":[{"source":"PubMed","id":"21164107","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
