Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4J7U

Crystal structure of human sepiapterin reductase in complex with sulfathiazole

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004757	molecular_function	sepiapterin reductase (NADP+) activity
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006729	biological_process	tetrahydrobiopterin biosynthetic process
A	0006809	biological_process	nitric oxide biosynthetic process
A	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
A	0016491	molecular_function	oxidoreductase activity
A	0050661	molecular_function	NADP binding
A	0070062	cellular_component	extracellular exosome
B	0004757	molecular_function	sepiapterin reductase (NADP+) activity
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006729	biological_process	tetrahydrobiopterin biosynthetic process
B	0006809	biological_process	nitric oxide biosynthetic process
B	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
B	0016491	molecular_function	oxidoreductase activity
B	0050661	molecular_function	NADP binding
B	0070062	cellular_component	extracellular exosome
C	0004757	molecular_function	sepiapterin reductase (NADP+) activity
C	0005737	cellular_component	cytoplasm
C	0005739	cellular_component	mitochondrion
C	0005829	cellular_component	cytosol
C	0006729	biological_process	tetrahydrobiopterin biosynthetic process
C	0006809	biological_process	nitric oxide biosynthetic process
C	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
C	0016491	molecular_function	oxidoreductase activity
C	0050661	molecular_function	NADP binding
C	0070062	cellular_component	extracellular exosome
D	0004757	molecular_function	sepiapterin reductase (NADP+) activity
D	0005737	cellular_component	cytoplasm
D	0005739	cellular_component	mitochondrion
D	0005829	cellular_component	cytosol
D	0006729	biological_process	tetrahydrobiopterin biosynthetic process
D	0006809	biological_process	nitric oxide biosynthetic process
D	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
D	0016491	molecular_function	oxidoreductase activity
D	0050661	molecular_function	NADP binding
D	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAP A 801

Chain	Residue
A	GLY11
A	ASP66
A	LEU67
A	ASN97
A	LEU123
A	ILE152
A	SER153
A	TYR167
A	LYS171
A	PRO195
A	GLY196
A	SER13
A	PRO197
A	LEU198
A	THR200
A	MET202
A	GLN203
A	YTZ802
A	HOH907
A	HOH918
A	HOH919
A	HOH921
A	ARG14
A	GLY15
A	PHE16
A	ALA38
A	ARG39
A	ASN40
A	ALA65

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE YTZ A 802

Chain	Residue
A	SER154
A	LEU155
A	PHE161
A	TYR167
A	GLY196
A	PRO197
A	GLN203
A	NAP801
A	PEG806
A	HOH905

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 A 803

Chain	Residue
A	ARG39

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 804

Chain	Residue
A	ARG59
D	ARG45

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PEG A 805

Chain	Residue
A	ASP254
A	PEG806
A	HOH943

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG A 806

Chain	Residue
A	GLY218
A	YTZ802
A	PEG805
A	HOH943

site_id	AC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAP B 801

Chain	Residue
B	GLY11
B	SER13
B	ARG14
B	GLY15
B	PHE16
B	ARG39
B	ASN40
B	ALA65
B	ASP66
B	LEU67
B	ASN97
B	ALA98
B	ILE152
B	SER153
B	TYR167
B	LYS171
B	PRO195
B	GLY196
B	PRO197
B	LEU198
B	THR200
B	MET202
B	GLN203
B	YTZ802
B	HOH906
B	HOH918

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE YTZ B 802

Chain	Residue
B	SER154
B	LEU155
B	PHE161
B	TRP164
B	TYR167
B	GLY196
B	PRO197
B	GLN203
B	NAP801
B	GOL805
B	HOH901

site_id	AC9
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 B 803

Chain	Residue
B	ARG39

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG B 804

Chain	Residue
B	ASP214
B	GOL805

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 805

Chain	Residue
B	ASP254
B	YTZ802
B	PEG804

site_id	BC3
Number of Residues	30
Details	BINDING SITE FOR RESIDUE NAP C 801

Chain	Residue
C	ALA65
C	ASP66
C	LEU67
C	ASN97
C	ALA98
C	LEU123
C	ILE152
C	SER153
C	TYR167
C	LYS171
C	PRO195
C	GLY196
C	PRO197
C	LEU198
C	THR200
C	MET202
C	GLN203
C	YTZ802
C	HOH901
C	HOH915
C	HOH917
C	HOH919
C	HOH942
C	GLY11
C	SER13
C	ARG14
C	GLY15
C	PHE16
C	ARG39
C	ASN40

site_id	BC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE YTZ C 802

Chain	Residue
C	SER154
C	LEU155
C	CYS156
C	PHE161
C	TYR167
C	GLY196
C	PRO197
C	GLN203
C	NAP801
C	PEG805
C	HOH902

site_id	BC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 C 803

Chain	Residue
C	ARG39

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 804

Chain	Residue
A	ARG45
C	ARG59

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG C 805

Chain	Residue
C	GLY218
C	YTZ802

site_id	BC8
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAP D 801

Chain	Residue
D	GLY11
D	SER13
D	ARG14
D	GLY15
D	PHE16
D	ARG39
D	ASN40
D	ALA65
D	ASP66
D	LEU67
D	ASN97
D	ALA98
D	LEU123
D	ILE152
D	SER153
D	TYR167
D	LYS171
D	PRO195
D	GLY196
D	PRO197
D	LEU198
D	THR200
D	MET202
D	GLN203
D	YTZ802

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE YTZ D 802

Chain	Residue
D	SER154
D	LEU155
D	TYR167
D	GLY196
D	PRO197
D	GLN203
D	NAP801
D	HOH914

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 D 803

Chain	Residue
D	ARG39

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	52
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human sepiapterin reductase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	20
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P18297","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by CaMK2; in vitro","evidences":[{"source":"PubMed","id":"11825621","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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