Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1DLA

NOVEL NADPH-BINDING DOMAIN REVEALED BY THE CRYSTAL STRUCTURE OF ALDOSE REDUCTASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001523	biological_process	retinoid metabolic process
A	0001758	molecular_function	retinal dehydrogenase activity
A	0004032	molecular_function	aldose reductase (NADPH) activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006693	biological_process	prostaglandin metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0036130	molecular_function	prostaglandin H2 endoperoxidase reductase activity
A	0042572	biological_process	retinol metabolic process
A	0047655	molecular_function	allyl-alcohol dehydrogenase activity
A	0047956	molecular_function	glycerol dehydrogenase [NADP+] activity
A	0052650	molecular_function	all-trans-retinol dehydrogenase (NADP+) activity
B	0001523	biological_process	retinoid metabolic process
B	0001758	molecular_function	retinal dehydrogenase activity
B	0004032	molecular_function	aldose reductase (NADPH) activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006693	biological_process	prostaglandin metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0036130	molecular_function	prostaglandin H2 endoperoxidase reductase activity
B	0042572	biological_process	retinol metabolic process
B	0047655	molecular_function	allyl-alcohol dehydrogenase activity
B	0047956	molecular_function	glycerol dehydrogenase [NADP+] activity
B	0052650	molecular_function	all-trans-retinol dehydrogenase (NADP+) activity
C	0001523	biological_process	retinoid metabolic process
C	0001758	molecular_function	retinal dehydrogenase activity
C	0004032	molecular_function	aldose reductase (NADPH) activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006629	biological_process	lipid metabolic process
C	0006693	biological_process	prostaglandin metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0036130	molecular_function	prostaglandin H2 endoperoxidase reductase activity
C	0042572	biological_process	retinol metabolic process
C	0047655	molecular_function	allyl-alcohol dehydrogenase activity
C	0047956	molecular_function	glycerol dehydrogenase [NADP+] activity
C	0052650	molecular_function	all-trans-retinol dehydrogenase (NADP+) activity
D	0001523	biological_process	retinoid metabolic process
D	0001758	molecular_function	retinal dehydrogenase activity
D	0004032	molecular_function	aldose reductase (NADPH) activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006629	biological_process	lipid metabolic process
D	0006693	biological_process	prostaglandin metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0036130	molecular_function	prostaglandin H2 endoperoxidase reductase activity
D	0042572	biological_process	retinol metabolic process
D	0047655	molecular_function	allyl-alcohol dehydrogenase activity
D	0047956	molecular_function	glycerol dehydrogenase [NADP+] activity
D	0052650	molecular_function	all-trans-retinol dehydrogenase (NADP+) activity

Functional Information from PROSITE/UniProt

site_id	PS00062
Number of Residues	18
Details	ALDOKETO_REDUCTASE_2 Aldo/keto reductase family signature 2. MeelvdeglVKAIGVSNF

Chain	Residue	Details
A	MET143-PHE160

site_id	PS00063
Number of Residues	16
Details	ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. IPKSVTpeRIaENfQV

Chain	Residue	Details
A	ILE259-VAL274

site_id	PS00798
Number of Residues	18
Details	ALDOKETO_REDUCTASE_1 Aldo/keto reductase family signature 1. GYRHIDCAhvyqnEneVG

Chain	Residue	Details
A	GLY37-GLY54

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250\|UniProtKB:P15121

Chain	Residue	Details
A	GLN48
B	GLN48
C	GLN48
D	GLN48

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	ALA9
B	ALA9
C	ALA9
D	ALA9

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	TRP110
B	TRP110
C	TRP110
D	TRP110

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P15121

Chain	Residue	Details
A	PRO210
B	PRO210
C	PRO210
D	PRO210

site_id	SWS_FT_FI5
Number of Residues	4
Details	SITE: Lowers pKa of active site Tyr => ECO:0000250

Chain	Residue	Details
A	LEU77
B	LEU77
C	LEU77
D	LEU77

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: N-acetylalanine => ECO:0000269\|PubMed:8281941

Chain	Residue	Details
A	SER1
B	SER1
C	SER1
D	SER1

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P07943

Chain	Residue	Details
A	HIS2
B	HIS2
C	HIS2
D	HIS2

site_id	SWS_FT_FI8
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P15121

Chain	Residue	Details
A	PRO221
A	SER262
B	PRO221
B	SER262
C	PRO221
C	SER262
D	PRO221
D	SER262

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