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4NTF

Mus Musculus LTC4 synthase in S-hexyl-GSH complex form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004464molecular_functionleukotriene-C4 synthase activity
A0004602molecular_functionglutathione peroxidase activity
A0005635cellular_componentnuclear envelope
A0005640cellular_componentnuclear outer membrane
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006691biological_processleukotriene metabolic process
A0008047molecular_functionenzyme activator activity
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
A0043295molecular_functionglutathione binding
A0044877molecular_functionprotein-containing complex binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GTX A 201
ChainResidue
ASER23
AARG90
ATYR93
AARG104
ALEU108
AALA112
ATRP116
AHOH301
AHOH302
AVAL26
AILE27
AARG30
APHE50
AGLN53
AASN55
AGLU58
ATYR59

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PLM A 202
ChainResidue
APHE74
AVAL128
APRO132
ALEU135
AARG136

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PLM A 203
ChainResidue
ATHR10
ALEU127
APHE130

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PLM A 204
ChainResidue
AGLN95

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PLM A 205
ChainResidue
ATHR10
AGLY77

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 206
ChainResidue
AARG48
AARG99
ASER100
ASER100
AALA101
AALA101
AGLN102

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NI A 207
ChainResidue
AHIS1
AHIS1
AHIS1

Functional Information from PROSITE/UniProt
site_idPS01297
Number of Residues15
DetailsFLAP_GST2_LTC4S FLAP/GST2/LTC4S family signature. GppeFERVFrAQvNC
ChainResidueDetails
AGLY42-CYS56

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues79
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"Q16873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues29
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"UniProtKB","id":"Q16873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"Q16873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q16873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q16873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q16873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q16873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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