Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3PCV

Crystal structure analysis of human leukotriene C4 synthase at 1.9 angstrom resolution

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	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	15
Details	BINDING SITE FOR RESIDUE GSH A 201

Chain	Residue
A	SER23
A	TYR93
A	TYR97
A	ARG104
A	LEU108
A	EDO217
A	HOH303
A	ILE27
A	ARG30
A	TYR50
A	ARG51
A	GLN53
A	ASN55
A	GLU58
A	TYR59

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LMT A 203

Chain	Residue
A	LEU7
A	LEU127
A	PHE130

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE LMT A 204

Chain	Residue
A	ALA20
A	TRP116
A	EDO217

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LMT A 205

Chain	Residue
A	LEU18
A	GLN95

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LMT A 206

Chain	Residue
A	PHE74
A	ALA128
A	PRO132
A	LEU135

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE LMT A 207

Chain	Residue
A	ALA10
A	GLY77
A	LEU81
A	LEU84

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LMT A 208

Chain	Residue
A	MET1
A	ILE72

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LMT A 209

Chain	Residue
A	TRP116
A	LEU117

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LMT A 211

Chain	Residue
A	LEU84
A	PHE88

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE LMT A 213

Chain	Residue
A	LEU18
A	PHE88

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 214

Chain	Residue
A	THR40
A	TYR50
A	TYR50
A	ARG51
A	HOH314

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 215

Chain	Residue
A	GLN19
A	SER23
A	SER57
A	GLU58
A	LEU62

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 216

Chain	Residue
A	SER36
A	ARG104
A	EDO217
A	HOH333
A	HOH381

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 217

Chain	Residue
A	GSH201
A	LMT204
A	EDO216
A	HOH382

site_id	BC6
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 250

Chain	Residue
A	SER100
A	SER100
A	ALA101
A	ALA101
A	GLN102
A	GLN102
A	HOH307
A	HOH307
A	HOH336

site_id	BC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 251

Chain	Residue
A	ARG34
A	ARG34
A	ARG34
A	HOH398
A	HOH398
A	HOH398

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	8
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_FI2
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_FI3
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_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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)