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4NTA

Mus Musculus LTC4 synthase in apo form

Functional Information from GO Data
ChainGOidnamespacecontents
A0004364molecular_functionglutathione transferase activity
A0004464molecular_functionleukotriene-C4 synthase activity
A0004602molecular_functionglutathione peroxidase activity
A0005634cellular_componentnucleus
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
A0043295molecular_functionglutathione binding
A0044877molecular_functionprotein-containing complex binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PLM A 201
ChainResidue
ALEU124
AVAL128
APRO132
ALEU135
AARG136

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PLM A 202
ChainResidue
ATHR10
APHE130

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE PLM A 203
ChainResidue
AGLN95

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PLM A 204
ChainResidue
AVAL14
AGLY77
ALEU81
ALEU84
ATHR10

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 205
ChainResidue
AILE27
AARG30
AARG51
AASN55
ATYR93
AARG104

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

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
DetailsTRANSMEM: Helical => ECO:0000250|UniProtKB:Q16873
ChainResidueDetails
ALEU7-ILE27
AVAL49-VAL69
APHE74-PHE94
ALEU105-LEU124

site_idSWS_FT_FI2
Number of Residues29
DetailsTOPO_DOM: Lumenal => ECO:0000250|UniProtKB:Q16873
ChainResidueDetails
ASER28-ARG48
AGLN95-ARG104

site_idSWS_FT_FI3
Number of Residues28
DetailsTOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:Q16873
ChainResidueDetails
AALA70-PHE73
AGLY125-ALA150

site_idSWS_FT_FI4
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q16873
ChainResidueDetails
AARG31

site_idSWS_FT_FI5
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q16873
ChainResidueDetails
AARG104

site_idSWS_FT_FI6
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q16873
ChainResidueDetails
AARG30
AARG51
AGLN53
AGLU58
ATYR93

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q16873
ChainResidueDetails
ASER36

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PDB entries from 2024-07-24

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