Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4HWK

Crystal structure of human sepiapterin reductase in complex with sulfapyridine

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	34
Details	BINDING SITE FOR RESIDUE NAP A 801

Chain	Residue
A	GLY11
A	ASP66
A	LEU67
A	ASN97
A	ALA98
A	LEU123
A	ILE152
A	SER153
A	TYR167
A	LYS171
A	PRO195
A	SER13
A	GLY196
A	PRO197
A	LEU198
A	THR200
A	MET202
A	GLN203
A	SFY807
A	HOH901
A	HOH902
A	HOH903
A	ARG14
A	HOH914
A	HOH921
A	HOH926
A	HOH937
A	HOH956
A	GLY15
A	PHE16
A	ALA38
A	ARG39
A	ASN40
A	ALA65

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 802

Chain	Residue
A	ARG39
A	HOH921
A	HOH991

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 803

Chain	Residue
A	LYS87
A	GLY88

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 804

Chain	Residue
A	GLY196
A	ASP254
A	SFY807
A	SO4808
A	HOH905
A	HOH1004

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 805

Chain	Residue
A	ARG45
A	ARG62

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 806

Chain	Residue
A	ASP199
A	GLY226
A	LEU228
C	ASP230
C	HOH967

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SFY A 807

Chain	Residue
A	SER154
A	LEU155
A	CYS156
A	PHE161
A	TRP164
A	TYR167
A	GLY196
A	PRO197
A	GLN203
A	NAP801
A	GOL804
A	PEG810
A	HOH905

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 808

Chain	Residue
A	TYR256
A	GOL804

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 809

Chain	Residue
A	GLY15
A	ASP201
A	HOH901
B	LYS87

site_id	BC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PEG A 810

Chain	Residue
A	SFY807
A	HOH1004

site_id	BC2
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAP B 801

Chain	Residue
B	HOH903
B	HOH908
B	HOH912
B	HOH914
B	HOH926
B	HOH931
B	HOH947
B	HOH969
B	GLY11
B	SER13
B	ARG14
B	GLY15
B	PHE16
B	ALA38
B	ARG39
B	ASN40
B	ALA65
B	ASP66
B	LEU67
B	ASN97
B	ALA98
B	LEU123
B	ILE152
B	SER153
B	TYR167
B	LYS171
B	PRO195
B	GLY196
B	PRO197
B	LEU198
B	THR200
B	MET202
B	GLN203
B	SFY806

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 802

Chain	Residue
B	ARG39
B	HOH931
B	HOH932

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL B 803

Chain	Residue
B	ASP254
B	SFY806

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 804

Chain	Residue
A	ARG45
B	ARG59
B	VAL60
B	HOH974

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 805

Chain	Residue
B	LYS87
B	GLY88

site_id	BC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE SFY B 806

Chain	Residue
B	SER154
B	LEU155
B	CYS156
B	PHE161
B	TRP164
B	TYR167
B	GLY196
B	PRO197
B	GLN203
B	NAP801
B	GOL803
B	GOL807
B	HOH905

site_id	BC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 807

Chain	Residue
B	MET215
B	GLY218
B	SFY806

site_id	BC9
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAP C 801

Chain	Residue
C	GLY11
C	SER13
C	ARG14
C	GLY15
C	PHE16
C	ALA38
C	ARG39
C	ASN40
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	SFY804
C	HOH901
C	HOH917
C	HOH931
C	HOH939
C	HOH940
C	HOH955
C	HOH956

site_id	CC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 802

Chain	Residue
C	ARG39
C	HOH955

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 803

Chain	Residue
C	GLY196
C	ASP254
C	SFY804
C	HOH902

site_id	CC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE SFY C 804

Chain	Residue
C	SER154
C	LEU155
C	CYS156
C	PHE161
C	TRP164
C	TYR167
C	GLY196
C	PRO197
C	GLN203
C	MET215
C	NAP801
C	GOL803
C	PEG805
C	HOH902

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PEG C 805

Chain	Residue
C	ASP214
C	MET215
C	SFY804
C	HOH973

site_id	CC5
Number of Residues	32
Details	BINDING SITE FOR RESIDUE NAP D 801

Chain	Residue
D	GLY11
D	SER13
D	ARG14
D	GLY15
D	PHE16
D	ALA38
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	SFY803
D	HOH904
D	HOH933
D	HOH937
D	HOH938
D	HOH941
D	HOH948

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 802

Chain	Residue
D	ARG39
D	HOH938

site_id	CC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SFY D 803

Chain	Residue
D	SER154
D	LEU155
D	CYS156
D	PHE161
D	TRP164
D	TYR167
D	GLY196
D	PRO197
D	GLN203
D	NAP801
D	HOH912

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 D 804

Chain	Residue
B	ARG55
D	ARG45
D	ARG62

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)