Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1V40

First Inhibitor Complex Structure of Human Hematopoietic Prostaglandin D Synthase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0001516	biological_process	prostaglandin biosynthetic process
A	0004364	molecular_function	glutathione transferase activity
A	0004667	molecular_function	prostaglandin-D synthase activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006693	biological_process	prostaglandin metabolic process
A	0006749	biological_process	glutathione metabolic process
A	0007165	biological_process	signal transduction
A	0007626	biological_process	locomotory behavior
A	0016740	molecular_function	transferase activity
A	0016853	molecular_function	isomerase activity
A	0042803	molecular_function	protein homodimerization activity
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0046872	molecular_function	metal ion binding
A	2000255	biological_process	negative regulation of male germ cell proliferation
B	0000287	molecular_function	magnesium ion binding
B	0001516	biological_process	prostaglandin biosynthetic process
B	0004364	molecular_function	glutathione transferase activity
B	0004667	molecular_function	prostaglandin-D synthase activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0006693	biological_process	prostaglandin metabolic process
B	0006749	biological_process	glutathione metabolic process
B	0007165	biological_process	signal transduction
B	0007626	biological_process	locomotory behavior
B	0016740	molecular_function	transferase activity
B	0016853	molecular_function	isomerase activity
B	0042803	molecular_function	protein homodimerization activity
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0046872	molecular_function	metal ion binding
B	2000255	biological_process	negative regulation of male germ cell proliferation
C	0000287	molecular_function	magnesium ion binding
C	0001516	biological_process	prostaglandin biosynthetic process
C	0004364	molecular_function	glutathione transferase activity
C	0004667	molecular_function	prostaglandin-D synthase activity
C	0005509	molecular_function	calcium ion binding
C	0005515	molecular_function	protein binding
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
C	0006693	biological_process	prostaglandin metabolic process
C	0006749	biological_process	glutathione metabolic process
C	0007165	biological_process	signal transduction
C	0007626	biological_process	locomotory behavior
C	0016740	molecular_function	transferase activity
C	0016853	molecular_function	isomerase activity
C	0042803	molecular_function	protein homodimerization activity
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0046872	molecular_function	metal ion binding
C	2000255	biological_process	negative regulation of male germ cell proliferation
D	0000287	molecular_function	magnesium ion binding
D	0001516	biological_process	prostaglandin biosynthetic process
D	0004364	molecular_function	glutathione transferase activity
D	0004667	molecular_function	prostaglandin-D synthase activity
D	0005509	molecular_function	calcium ion binding
D	0005515	molecular_function	protein binding
D	0005654	cellular_component	nucleoplasm
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006633	biological_process	fatty acid biosynthetic process
D	0006693	biological_process	prostaglandin metabolic process
D	0006749	biological_process	glutathione metabolic process
D	0007165	biological_process	signal transduction
D	0007626	biological_process	locomotory behavior
D	0016740	molecular_function	transferase activity
D	0016853	molecular_function	isomerase activity
D	0042803	molecular_function	protein homodimerization activity
D	0043231	cellular_component	intracellular membrane-bounded organelle
D	0046872	molecular_function	metal ion binding
D	2000255	biological_process	negative regulation of male germ cell proliferation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 3900

Chain	Residue
A	HOH4129
A	HOH4174
A	HOH4290
D	HOH3999
D	HOH4095
D	HOH4096

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 3901

Chain	Residue
C	HOH3625
C	HOH3663
C	HOH3812
B	HOH4013
B	HOH4141
B	HOH4142

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GSH A 3200

Chain	Residue
A	TYR8
A	ARG14
A	TRP39
A	LYS43
A	LYS50
A	ILE51
A	GLN63
A	SER64
A	O163201
A	HOH3953
A	HOH3959
A	HOH4117
A	HOH4289
D	ASP697

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GSH B 3400

Chain	Residue
B	TYR208
B	ARG214
B	TRP239
B	LYS243
B	LYS250
B	ILE251
B	GLN263
B	SER264
B	O163401
B	HOH3950
B	HOH4010
B	HOH4155
C	ASP497

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE GSH C 3600

Chain	Residue
B	ASP297
C	TYR408
C	ARG414
C	TRP439
C	LYS443
C	LYS450
C	ILE451
C	GLN463
C	SER464
C	O163601
C	HOH3623
C	HOH3664
C	HOH3665
C	HOH3852

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GSH D 3800

Chain	Residue
A	ASP97
D	TYR608
D	ARG614
D	TRP639
D	LYS643
D	LYS650
D	ILE651
D	GLN663
D	SER664
D	HOH3822
D	HOH3867
D	HOH3872
D	HOH4058

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE O16 A 3201

Chain	Residue
A	PHE9
A	ARG14
A	MET99
A	TRP104
A	ALA105
A	TYR152
A	CYS156
A	LEU199
A	GSH3200

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE O16 B 3401

Chain	Residue
B	PHE209
B	GLY213
B	MET299
B	TRP304
B	ALA305
B	TYR352
B	CYS356
B	GSH3400
B	HOH3917

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE O16 C 3601

Chain	Residue
C	PHE409
C	GLY413
C	ARG414
C	ASP496
C	MET499
C	TRP504
C	ALA505
C	TYR552
C	CYS556
C	LEU599
C	GSH3600

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE O16 D 3801

Chain	Residue
D	MET699
D	TRP704
D	ALA705
D	TYR752
D	LEU799
D	HOH4090
A	HOH4258
D	GLY613
D	ARG614
D	ASP696

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 3001

Chain	Residue
A	LYS43
A	PHE48
A	GLY49
A	HOH3991
A	HOH4119
A	HOH4126
A	HOH4287
D	HIS726
D	ASP730
D	HOH3804

site_id	BC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL A 3002

Chain	Residue
A	GLU84
A	TYR134
A	ARG138
A	LEU141
A	ILE142
A	GLY143
A	HOH4029
A	HOH4142
A	HOH4260
A	HOH4311
D	TYR722

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C 3003

Chain	Residue
C	GLN428
C	TYR429
D	GLN796
D	THR797
D	LYS798
D	HOH3904
D	HOH3905
D	HOH3991
D	HOH3992
D	HOH3993

site_id	BC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 3004

Chain	Residue
C	THR597
C	HOH3735
C	HOH3737
C	HOH3741
C	HOH3744
C	HOH3745
D	GLN628
D	TYR629
D	GOL3005

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL D 3005

Chain	Residue
C	LYS598
C	GOL3004
D	GLN628
D	TYR629
D	TRP790
D	HOH3891
D	HOH3892

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 3006

Chain	Residue
B	GLN228
B	TYR229

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:12627223, ECO:0000269\|PubMed:15113825, ECO:0000269\|PubMed:16547010, ECO:0000269\|PubMed:18341273, ECO:0000269\|PubMed:19939518

Chain	Residue	Details
A	PHE9
B	SER264
C	PHE409
C	ALA415
C	PRO440
C	LYS450
C	SER464
D	PHE609
D	ALA615
D	PRO640
D	LYS650
A	ALA15
D	SER664
A	PRO40
A	LYS50
A	SER64
B	PHE209
B	ALA215
B	PRO240
B	LYS250

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