Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4Z3K

Human sepiapterin reductase in complex with the cofactor NADP+ and the trypthophan metabolite xanthurenic acid

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	32
Details	binding site for residue NAP A 801

Chain	Residue
A	GLY11
A	ASP66
A	LEU67
A	ASN97
A	ALA98
A	GLY99
A	LEU123
A	ILE152
A	SER153
A	TYR167
A	LYS171
A	SER13
A	PRO195
A	GLY196
A	PRO197
A	LEU198
A	THR200
A	ASP201
A	MET202
A	GLN203
A	4KL802
A	HOH907
A	ARG14
A	HOH910
A	HOH917
A	HOH930
A	GLY15
A	PHE16
A	ALA38
A	ARG39
A	ASN40
A	ALA65

site_id	AC2
Number of Residues	10
Details	binding site for residue 4KL A 802

Chain	Residue
A	SER154
A	LEU155
A	TRP164
A	TYR167
A	GLN203
A	LEU219
A	NAP801
A	HOH901
A	HOH908
A	HOH915

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	29
Details	binding site for residue NAP B 301

Chain	Residue
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	GLY99
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	4KL302
B	HOH406
B	HOH410

site_id	AC5
Number of Residues	11
Details	binding site for residue 4KL B 302

Chain	Residue
B	SER154
B	LEU155
B	TRP164
B	TYR167
B	PRO197
B	GLN203
B	NAP301
B	HOH401
B	HOH402
B	HOH403
B	HOH418

site_id	AC6
Number of Residues	2
Details	binding site for residue SO4 B 303

Chain	Residue
C	LYS87
C	GLY88

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 B 304

Chain	Residue
B	ARG39
B	HOH413
B	HOH427

site_id	AC8
Number of Residues	2
Details	binding site for residue EDO B 305

Chain	Residue
B	LYS217
B	GLN220

site_id	AC9
Number of Residues	29
Details	binding site for residue NAP C 301

Chain	Residue
C	ASP66
C	LEU67
C	ASN97
C	ILE152
C	SER153
C	TYR167
C	LYS171
C	PRO195
C	GLY196
C	PRO197
C	LEU198
C	THR200
C	ASP201
C	MET202
C	GLN203
C	4KL302
C	HOH409
C	HOH413
C	HOH415
C	HOH431
C	GLY11
C	SER13
C	ARG14
C	GLY15
C	PHE16
C	ALA38
C	ARG39
C	ASN40
C	ALA65

site_id	AD1
Number of Residues	12
Details	binding site for residue 4KL C 302

Chain	Residue
C	SER154
C	LEU155
C	TRP164
C	TYR167
C	PRO197
C	GLN203
C	LEU219
C	NAP301
C	SO4304
C	HOH401
C	HOH405
C	HOH410

site_id	AD2
Number of Residues	1
Details	binding site for residue SO4 C 303

Chain	Residue
C	ARG39

site_id	AD3
Number of Residues	6
Details	binding site for residue SO4 C 304

Chain	Residue
C	CYS156
C	PHE161
C	TRP164
C	MET215
C	4KL302
C	HOH401

site_id	AD4
Number of Residues	30
Details	binding site for residue NAP D 301

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	GLY99
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	4KL302
D	HOH410
D	HOH427
D	HOH429

site_id	AD5
Number of Residues	12
Details	binding site for residue 4KL D 302

Chain	Residue
D	SER154
D	LEU155
D	TRP164
D	TYR167
D	PRO197
D	GLN203
D	NAP301
D	SO4303
D	HOH401
D	HOH403
D	HOH408
D	HOH422

site_id	AD6
Number of Residues	5
Details	binding site for residue SO4 D 303

Chain	Residue
D	CYS156
D	PHE161
D	TRP164
D	MET215
D	4KL302

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)