Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1DIR

CRYSTAL STRUCTURE OF A MONOCLINIC FORM OF DIHYDROPTERIDINE REDUCTASE FROM RAT LIVER

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001889	biological_process	liver development
A	0004155	molecular_function	6,7-dihydropteridine reductase activity
A	0005737	cellular_component	cytoplasm
A	0006559	biological_process	L-phenylalanine catabolic process
A	0006729	biological_process	tetrahydrobiopterin biosynthetic process
A	0010044	biological_process	response to aluminum ion
A	0010288	biological_process	response to lead ion
A	0016491	molecular_function	oxidoreductase activity
A	0033762	biological_process	response to glucagon
A	0042558	biological_process	pteridine-containing compound metabolic process
A	0042802	molecular_function	identical protein binding
A	0070402	molecular_function	NADPH binding
A	0070404	molecular_function	NADH binding
A	0071466	biological_process	cellular response to xenobiotic stimulus
B	0001889	biological_process	liver development
B	0004155	molecular_function	6,7-dihydropteridine reductase activity
B	0005737	cellular_component	cytoplasm
B	0006559	biological_process	L-phenylalanine catabolic process
B	0006729	biological_process	tetrahydrobiopterin biosynthetic process
B	0010044	biological_process	response to aluminum ion
B	0010288	biological_process	response to lead ion
B	0016491	molecular_function	oxidoreductase activity
B	0033762	biological_process	response to glucagon
B	0042558	biological_process	pteridine-containing compound metabolic process
B	0042802	molecular_function	identical protein binding
B	0070402	molecular_function	NADPH binding
B	0070404	molecular_function	NADH binding
B	0071466	biological_process	cellular response to xenobiotic stimulus
C	0001889	biological_process	liver development
C	0004155	molecular_function	6,7-dihydropteridine reductase activity
C	0005737	cellular_component	cytoplasm
C	0006559	biological_process	L-phenylalanine catabolic process
C	0006729	biological_process	tetrahydrobiopterin biosynthetic process
C	0010044	biological_process	response to aluminum ion
C	0010288	biological_process	response to lead ion
C	0016491	molecular_function	oxidoreductase activity
C	0033762	biological_process	response to glucagon
C	0042558	biological_process	pteridine-containing compound metabolic process
C	0042802	molecular_function	identical protein binding
C	0070402	molecular_function	NADPH binding
C	0070404	molecular_function	NADH binding
C	0071466	biological_process	cellular response to xenobiotic stimulus
D	0001889	biological_process	liver development
D	0004155	molecular_function	6,7-dihydropteridine reductase activity
D	0005737	cellular_component	cytoplasm
D	0006559	biological_process	L-phenylalanine catabolic process
D	0006729	biological_process	tetrahydrobiopterin biosynthetic process
D	0010044	biological_process	response to aluminum ion
D	0010288	biological_process	response to lead ion
D	0016491	molecular_function	oxidoreductase activity
D	0033762	biological_process	response to glucagon
D	0042558	biological_process	pteridine-containing compound metabolic process
D	0042802	molecular_function	identical protein binding
D	0070402	molecular_function	NADPH binding
D	0070404	molecular_function	NADH binding
D	0071466	biological_process	cellular response to xenobiotic stimulus

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD A 241

Chain	Residue
A	TYR12
A	ALA83
A	GLY84
A	GLY85
A	LYS105
A	GLN106
A	THR110
A	ALA131
A	TYR146
A	LYS150
A	PRO178
A	GLY13
A	VAL179
A	THR180
A	LEU181
A	ASN186
A	HOH959
A	HOH974
A	GLY16
A	ALA17
A	LEU18
A	ASP37
A	VAL50
A	GLN59
A	VAL82

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD B 241

Chain	Residue
B	TYR12
B	GLY13
B	GLY16
B	LEU18
B	ASP37
B	VAL38
B	VAL50
B	GLN59
B	VAL82
B	ALA83
B	GLY84
B	GLY85
B	LYS105
B	GLN106
B	THR110
B	ALA131
B	GLY132
B	TYR146
B	LYS150
B	PRO178
B	VAL179
B	LEU181
B	ASN186
B	HOH977

site_id	AC3
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD C 241

Chain	Residue
C	TYR12
C	GLY13
C	ARG15
C	GLY16
C	ALA17
C	LEU18
C	ASP37
C	VAL38
C	VAL50
C	GLN59
C	VAL82
C	ALA83
C	GLY84
C	GLY85
C	LYS105
C	GLN106
C	THR110
C	ALA131
C	TYR146
C	LYS150
C	PRO178
C	VAL179
C	LEU181
C	ASN186

site_id	AC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE NAD D 241

Chain	Residue
D	TYR12
D	GLY13
D	GLY16
D	ALA17
D	LEU18
D	ASP37
D	VAL82
D	ALA83
D	GLY84
D	GLY85
D	GLN106
D	THR110
D	TYR146
D	LYS150
D	PRO178
D	VAL179
D	LEU181
D	ASN186
D	HOH972
D	HOH973

Functional Information from PROSITE/UniProt

site_id	PS00061
Number of Residues	29
Details	ADH_SHORT Short-chain dehydrogenases/reductases family signature. AkaaldgtpgMigYGMAKGAVhQLCqSLA

Chain	Residue	Details
A	ALA133-ALA161

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	96
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8BVI4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
A	ASN186
A	TYR146
A	LYS150

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
B	TYR146
B	LYS150

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
C	TYR146
C	LYS150

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
D	TYR146
D	LYS150

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
B	ASN186
B	TYR146
B	LYS150

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
C	ASN186
C	TYR146
C	LYS150

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
D	ASN186
D	TYR146
D	LYS150

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
A	MET143
A	LYS150

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
B	MET143
B	LYS150

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
C	MET143
C	LYS150

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
D	MET143
D	LYS150

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1dhr

Chain	Residue	Details
A	TYR146
A	LYS150

site_id	MCSA1
Number of Residues	2
Details	M-CSA 491

Chain	Residue	Details
A	TYR146	electrostatic stabiliser, proton shuttle (general acid/base)
A	LYS150	electrostatic stabiliser, proton shuttle (general acid/base)

site_id	MCSA2
Number of Residues	2
Details	M-CSA 491

Chain	Residue	Details
B	TYR146	electrostatic stabiliser, proton shuttle (general acid/base)
B	LYS150	electrostatic stabiliser, proton shuttle (general acid/base)

site_id	MCSA3
Number of Residues	2
Details	M-CSA 491

Chain	Residue	Details
C	TYR146	electrostatic stabiliser, proton shuttle (general acid/base)
C	LYS150	electrostatic stabiliser, proton shuttle (general acid/base)

site_id	MCSA4
Number of Residues	2
Details	M-CSA 491

Chain	Residue	Details
D	TYR146	electrostatic stabiliser, proton shuttle (general acid/base)
D	LYS150	electrostatic stabiliser, proton shuttle (general acid/base)

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