9D6Y

Crystal structure of Apo Human Prostaglandin reductase 1 (PTGR1) (Orthorhombic C form)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006691	biological_process	leukotriene metabolic process
A	0006693	biological_process	prostaglandin metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0032440	molecular_function	2-alkenal reductase [NAD(P)H] activity
A	0035798	molecular_function	2-alkenal reductase (NADPH) activity
A	0036102	biological_process	leukotriene B4 metabolic process
A	0036185	molecular_function	13-lipoxin reductase activity
A	0047522	molecular_function	15-oxoprostaglandin 13-reductase [NAD(P)+] activity
A	0070062	cellular_component	extracellular exosome
A	0097257	molecular_function	leukotriene B4 12-hydroxy dehydrogenase activity
A	2001302	biological_process	lipoxin A4 metabolic process
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006691	biological_process	leukotriene metabolic process
B	0006693	biological_process	prostaglandin metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0032440	molecular_function	2-alkenal reductase [NAD(P)H] activity
B	0035798	molecular_function	2-alkenal reductase (NADPH) activity
B	0036102	biological_process	leukotriene B4 metabolic process
B	0036185	molecular_function	13-lipoxin reductase activity
B	0047522	molecular_function	15-oxoprostaglandin 13-reductase [NAD(P)+] activity
B	0070062	cellular_component	extracellular exosome
B	0097257	molecular_function	leukotriene B4 12-hydroxy dehydrogenase activity
B	2001302	biological_process	lipoxin A4 metabolic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of human leukotriene B4 12-hydroxydehydrogenase in complex with NADP and raloxifene.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91YR9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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