4JRZ

Human LTC4 synthase in complex with product analogs - implications for enzyme catalysis

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	6
Details	BINDING SITE FOR RESIDUE NI A 201

Chain	Residue
A	HIS-1
A	HIS-1
A	HIS-1
A	HIS1
A	HIS1
A	HIS1

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NI A 202

Chain	Residue
A	HIS-4
A	HIS-4
A	HIS-2
A	HIS-4
A	HIS-2
A	HIS-2

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NI A 203

Chain	Residue
A	HIS-1
A	HIS-2
A	HIS-3
A	HOH317

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 204

Chain	Residue
A	SER100
A	SER100
A	ALA101
A	ALA101
A	GLN102
A	GLN102
A	HOH301
A	HOH301
A	HOH303
A	HOH303

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PAM A 205

Chain	Residue
A	HIS0
A	HIS1
A	LYS2
A	GLU4
A	TRP68
A	ILE72
A	HOH310
A	HOH314

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PLM A 206

Chain	Residue
A	PHE74
A	ALA128
A	LEU135
A	ARG136

---

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PLM A 207

Chain	Residue
A	LEU127
A	PHE130

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PLM A 208

Chain	Residue
A	TYR21
A	GLN95

---

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PLM A 209

Chain	Residue
A	LEU81

---

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PLM A 210

Chain	Residue
A	LEU131

---

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GTX A 211

Chain	Residue
A	SER23
A	VAL26
A	ILE27
A	ARG30
A	TYR50
A	GLN53
A	ASN55
A	GLU58
A	TYR59
A	TYR93
A	ARG104
A	LEU108
A	ALA112
A	PHE116

---

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	Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"12023288","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632546","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	29
Details	Topological 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"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	28
Details	Topological 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"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17632546","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27365393","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	9
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17632548","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by RPS6KB1","evidences":[{"source":"PubMed","id":"27365393","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---