2UUI

Crystal structure of Human Leukotriene C4 Synthase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004364	molecular_function	glutathione transferase activity
A	0004464	molecular_function	leukotriene-C4 synthase activity
A	0004602	molecular_function	glutathione peroxidase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005635	cellular_component	nuclear envelope
A	0005640	cellular_component	nuclear outer membrane
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006629	biological_process	lipid metabolic process
A	0006691	biological_process	leukotriene metabolic process
A	0008047	molecular_function	enzyme activator activity
A	0008289	molecular_function	lipid binding
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0016829	molecular_function	lyase activity
A	0019370	biological_process	leukotriene biosynthetic process
A	0031965	cellular_component	nuclear membrane
A	0042759	biological_process	long-chain fatty acid biosynthetic process
A	0042802	molecular_function	identical protein binding
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0046394	biological_process	carboxylic acid biosynthetic process
A	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NI A1151

Chain	Residue
A	HIS-1
A	HIS1

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NI A1152

Chain	Residue
A	HIS-4
A	HIS-2

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NI A1153

Chain	Residue
A	HIS-2
A	HOH2001

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LMT A1154

Chain	Residue
A	LMT1155
A	TYR109
A	ARG113
A	TRP116

---

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE LMT A1155

Chain	Residue
A	ILE27
A	ARG31
A	ARG104
A	LEU108
A	TYR109
A	TRP116
A	LMT1154
A	PLM1160
A	SO41165
A	HOH2101
A	HOH2102
A	HOH2105

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PLM A1170

Chain	Residue
A	PRO132
A	LEU135

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PLM A1171

Chain	Residue
A	LEU84

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PLM A1173

Chain	Residue
A	LEU14
A	GLY77
A	LEU81
A	LEU84

---

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PLM A1156

Chain	Residue
A	LEU18
A	GLN95
A	HOH2016

---

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PLM A1157

Chain	Residue
A	LEU7
A	PHE130
A	PLM1159
A	PLM1161
A	HOH2087

---

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PLM A1158

Chain	Residue
A	LEU14
A	PHE88

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PLM A1159

Chain	Residue
A	LEU13
A	PHE130
A	PLM1157

---

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PLM A1175

Chain	Residue
A	ARG99
A	GLN102

---

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PLM A1160

Chain	Residue
A	LMT1155

---

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PLM A1161

Chain	Residue
A	HIS75
A	GLU76
A	GLY77
A	ARG144
A	PLM1157
A	PLM1162
A	PLM1163
A	HOH2062
A	HOH2064

---

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PLM A1162

Chain	Residue
A	GLU4
A	GLY71
A	ILE72
A	PLM1161
A	PLM1163
A	HOH2008
A	HOH2106

---

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PLM A1163

Chain	Residue
A	HIS0
A	LYS2
A	HIS75
A	ARG136
A	PLM1161
A	PLM1162

---

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A1164

Chain	Residue
A	SER100
A	ALA101
A	GLN102
A	HOH2108

---

site_id	CC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 A1165

Chain	Residue
A	ASN55
A	TYR93
A	ARG104
A	LEU108
A	LMT1155
A	HOH2102
A	HOH2109
A	HOH2110

---

Functional Information from PROSITE/UniProt

site_id	PS01297
Number of Residues	15
Details	FLAP_GST2_LTC4S FLAP/GST2/LTC4S family signature. GppeFERVYrAQvNC

Chain	Residue	Details
A	GLY42-CYS56

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	79
Details	TRANSMEM: Helical => ECO:0000305|PubMed:12023288, ECO:0000305|PubMed:17632546, ECO:0000305|PubMed:17632548

Chain	Residue	Details
A	LEU7-ILE27
A	VAL49-VAL69
A	PHE74-PHE94
A	LEU105-LEU124

---

site_id	SWS_FT_FI2
Number of Residues	29
Details	TOPO_DOM: Lumenal => ECO:0000305|PubMed:12023288, ECO:0000305|PubMed:17632546, ECO:0000305|PubMed:17632548

Chain	Residue	Details
A	SER28-ARG48
A	GLN95-ARG104

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	TOPO_DOM: Cytoplasmic => ECO:0000305|PubMed:12023288, ECO:0000305|PubMed:17632546, ECO:0000305|PubMed:17632548

Chain	Residue	Details
A	ALA70-PHE73
A	GLY125-ALA150

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:17632548

Chain	Residue	Details
A	ARG31

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:17632548

Chain	Residue	Details
A	ARG104

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:17632546, ECO:0000269|PubMed:17632548, ECO:0000269|PubMed:27365393

Chain	Residue	Details
A	ARG30

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:17632548

Chain	Residue	Details
A	ARG51
A	GLU58
A	TYR93

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphoserine; by RPS6KB1 => ECO:0000269|PubMed:27365393

Chain	Residue	Details
A	SER36

---