5AM2

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	10
Details	BINDING SITE FOR RESIDUE SO4 A 1548

Chain	Residue
A	LEU228
A	HOH2475
A	ARG440
A	MET441
A	VAL442
A	THR443
A	GLU446
A	HOH2115
A	HOH2279
A	HOH2280

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 1549

Chain	Residue
A	TRP336
A	MET339
A	PHE381
A	GLN384
A	HOH2328

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS A 1550

Chain	Residue
A	LYS144
A	PHE147
A	HOH2139

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG A 1551

Chain	Residue
A	ILE305
A	GLN388
A	ARG467

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE KUF A 1552

Chain	Residue
A	PHE267
A	TYR383
A	PHE387
A	LEU408
A	LEU428
A	KUF1553
A	HOH2271

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE KUF A 1553

Chain	Residue
A	LEU408
A	ASP496
A	PHE497
A	VAL498
A	HIS524
A	TRP525
A	KUF1552
A	HOH2424

---

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE KUF A 1554

Chain	Residue
A	TRP336
A	TYR343
A	MET469
A	ASN472
A	KUF1555
A	HOH2400
A	HOH2401

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE KUF A 1555

Chain	Residue
A	ILE363
A	PRO371
A	SER374
A	KUF1554

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
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_FI2
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_FI3
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_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15096040","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
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_FI6
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_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P34914","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
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_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P34914","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
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

---