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9G0V

Human LTC4 synthase in complex with compound 1

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004464molecular_functionleukotriene-C4 synthase activity
A0004602molecular_functionglutathione peroxidase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005640cellular_componentnuclear outer membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006691biological_processleukotriene metabolic process
A0008289molecular_functionlipid binding
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016829molecular_functionlyase activity
A0019370biological_processleukotriene biosynthetic process
A0031965cellular_componentnuclear membrane
A0042759biological_processlong-chain fatty acid biosynthetic process
A0042802molecular_functionidentical protein binding
A0043231cellular_componentintracellular membrane-bounded organelle
A0046394biological_processcarboxylic acid biosynthetic process
A0098869biological_processcellular oxidant detoxification
Functional Information from PROSITE/UniProt
site_idPS01297
Number of Residues15
DetailsFLAP_GST2_LTC4S FLAP/GST2/LTC4S family signature. GppeFERVYrAQvNC
ChainResidueDetails
AGLY42-CYS56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues79
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"12023288","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632546","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues29
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"12023288","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632546","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"12023288","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632546","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17632546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27365393","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by RPS6KB1","evidences":[{"source":"PubMed","id":"27365393","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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