Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6USN

Co-crystal structure of SPR with compound 5

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 301

Chain	Residue
A	GLY11
A	ALA65
A	ASP66
A	LEU67
A	ASN97
A	LEU123
A	ILE152
A	SER153
A	TYR167
A	LYS171
A	PRO195
A	ALA12
A	GLY196
A	LEU198
A	THR200
A	MET202
A	GLN203
A	GOL308
A	QGV310
A	HOH406
A	HOH410
A	HOH418
A	SER13
A	HOH424
A	HOH430
A	HOH442
A	ARG14
A	GLY15
A	PHE16
A	ALA38
A	ARG39
A	ASN40

site_id	AC2
Number of Residues	2
Details	binding site for residue SO4 A 302

Chain	Residue
A	ARG39
A	HOH416

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 303

Chain	Residue
A	ARG189
A	LYS248
A	SER249
A	HOH439

site_id	AC4
Number of Residues	2
Details	binding site for residue SO4 A 304

Chain	Residue
A	ARG45
A	ARG62

site_id	AC5
Number of Residues	2
Details	binding site for residue SO4 A 305

Chain	Residue
A	LYS87
A	GLY88

site_id	AC6
Number of Residues	2
Details	binding site for residue GOL A 306

Chain	Residue
A	GLU70
A	ALA71

site_id	AC7
Number of Residues	4
Details	binding site for residue GOL A 307

Chain	Residue
A	LYS232
B	LYS87
B	GLY88
C	LYS223

site_id	AC8
Number of Residues	4
Details	binding site for residue GOL A 308

Chain	Residue
A	ARG14
A	ARG39
A	ASN40
A	NAP301

site_id	AC9
Number of Residues	2
Details	binding site for residue PEG A 309

Chain	Residue
A	GLY218
A	QGV310

site_id	AD1
Number of Residues	10
Details	binding site for residue QGV A 310

Chain	Residue
A	SER154
A	LEU155
A	PHE161
A	TRP164
A	TYR167
A	GLN203
A	MET215
A	NAP301
A	PEG309
A	HOH431

site_id	AD2
Number of Residues	32
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	LEU123
B	ILE152
B	SER153
B	TYR167
B	LYS171
B	PRO195
B	GLY196
B	PRO197
B	LEU198
B	THR200
B	MET202
B	GLN203
B	QGV308
B	HOH402
B	HOH419
B	HOH428
B	HOH429
B	HOH436
B	HOH439

site_id	AD3
Number of Residues	1
Details	binding site for residue SO4 B 302

Chain	Residue
B	ARG39

site_id	AD4
Number of Residues	2
Details	binding site for residue SO4 B 303

Chain	Residue
A	ARG45
B	ARG59

site_id	AD5
Number of Residues	3
Details	binding site for residue SO4 B 304

Chain	Residue
B	ARG189
B	LYS248
B	SER249

site_id	AD6
Number of Residues	2
Details	binding site for residue SO4 B 305

Chain	Residue
B	GLU70
B	HOH404

site_id	AD7
Number of Residues	4
Details	binding site for residue GOL B 306

Chain	Residue
A	GLY15
A	ASP201
A	HOH429
B	LYS87

site_id	AD8
Number of Residues	2
Details	binding site for residue PEG B 307

Chain	Residue
B	GLY218
B	QGV308

site_id	AD9
Number of Residues	9
Details	binding site for residue QGV B 308

Chain	Residue
B	SER154
B	LEU155
B	TRP164
B	TYR167
B	GLN203
B	MET215
B	NAP301
B	PEG307
B	HOH431

site_id	AE1
Number of Residues	32
Details	binding site for residue NAP C 301

Chain	Residue
C	GLY11
C	ALA12
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	GLY99
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	QGV307
C	HOH414
C	HOH415
C	HOH418
C	HOH421

site_id	AE2
Number of Residues	1
Details	binding site for residue SO4 C 302

Chain	Residue
C	ARG39

site_id	AE3
Number of Residues	1
Details	binding site for residue SO4 C 303

Chain	Residue
C	GLN220

site_id	AE4
Number of Residues	3
Details	binding site for residue SO4 C 304

Chain	Residue
C	ARG189
C	LYS248
C	SER249

site_id	AE5
Number of Residues	3
Details	binding site for residue GOL C 305

Chain	Residue
C	ALA69
C	GLU70
C	ALA71

site_id	AE6
Number of Residues	4
Details	binding site for residue PEG C 306

Chain	Residue
C	ASP214
C	MET215
C	GLY218
C	QGV307

site_id	AE7
Number of Residues	9
Details	binding site for residue QGV C 307

Chain	Residue
C	SER154
C	LEU155
C	TRP164
C	TYR167
C	GLN203
C	MET215
C	NAP301
C	PEG306
C	HOH412

site_id	AE8
Number of Residues	30
Details	binding site for residue NAP D 301

Chain	Residue
D	GLY11
D	ALA12
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	LEU198
D	THR200
D	ASP201
D	MET202
D	GLN203
D	QGV309
D	HOH404
D	HOH415
D	HOH418
D	HOH422

site_id	AE9
Number of Residues	3
Details	binding site for residue SO4 D 302

Chain	Residue
B	GLU54
D	ARG45
D	ARG62

site_id	AF1
Number of Residues	1
Details	binding site for residue SO4 D 303

Chain	Residue
D	ARG39

site_id	AF2
Number of Residues	2
Details	binding site for residue SO4 D 304

Chain	Residue
A	ARG59
D	ARG45

site_id	AF3
Number of Residues	3
Details	binding site for residue SO4 D 305

Chain	Residue
A	LYS87
D	ARG14
D	GLY15

site_id	AF4
Number of Residues	1
Details	binding site for residue SO4 D 306

Chain	Residue
D	ARG216

site_id	AF5
Number of Residues	4
Details	binding site for residue SO4 D 307

Chain	Residue
D	ARG189
D	PHE247
D	LYS248
D	SER249

site_id	AF6
Number of Residues	2
Details	binding site for residue SO4 D 308

Chain	Residue
D	PRO143
D	GLY144

site_id	AF7
Number of Residues	7
Details	binding site for residue QGV D 309

Chain	Residue
D	SER154
D	LEU155
D	TRP164
D	TYR167
D	GLN203
D	MET215
D	NAP301

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)