Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3V35

Aldose reductase complexed with a nitro compound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001523	biological_process	retinoid metabolic process
A	0001758	molecular_function	retinal dehydrogenase (NAD+) activity
A	0004032	molecular_function	aldose reductase (NADPH) activity
A	0005515	molecular_function	protein binding
A	0005615	cellular_component	extracellular space
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate metabolic process
A	0006060	biological_process	sorbitol metabolic process
A	0006629	biological_process	lipid metabolic process
A	0006693	biological_process	prostaglandin metabolic process
A	0006700	biological_process	C21-steroid hormone biosynthetic process
A	0009055	molecular_function	electron transfer activity
A	0016491	molecular_function	oxidoreductase activity
A	0036130	molecular_function	prostaglandin H2 endoperoxidase reductase activity
A	0042572	biological_process	retinol metabolic process
A	0043795	molecular_function	glyceraldehyde oxidoreductase activity
A	0044597	biological_process	daunorubicin metabolic process
A	0044598	biological_process	doxorubicin metabolic process
A	0046370	biological_process	fructose biosynthetic process
A	0047655	molecular_function	allyl-alcohol dehydrogenase activity
A	0047939	molecular_function	L-glucuronate reductase activity
A	0047956	molecular_function	glycerol dehydrogenase (NADP+) activity
A	0052650	molecular_function	all-trans-retinol dehydrogenase (NADP+) activity
A	0070062	cellular_component	extracellular exosome
A	0071475	biological_process	cellular hyperosmotic salinity response

Functional Information from PDB Data

site_id	AC1
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAP A 316

Chain	Residue
A	GLY18
A	ASN160
A	GLN183
A	TYR209
A	SER210
A	PRO211
A	LEU212
A	GLY213
A	SER214
A	PRO215
A	ASP216
A	THR19
A	ALA245
A	ILE260
A	PRO261
A	LYS262
A	SER263
A	VAL264
A	THR265
A	ARG268
A	GLU271
A	ASN272
A	TRP20
A	DMF318
A	HOH402
A	HOH423
A	HOH466
A	LYS21
A	ASP43
A	TYR48
A	LYS77
A	HIS110
A	SER159

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE NTI A 317

Chain	Residue
A	TRP20
A	VAL47
A	TRP79
A	HIS110
A	TRP111
A	PRO218
A	TRP219
A	DMF318
A	DMF322
A	DMF329
A	DMF331
A	DMF332
A	DMF337
A	HOH430

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMF A 318

Chain	Residue
A	TRP20
A	TYR48
A	HIS110
A	TRP111
A	NAP316
A	NTI317

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMF A 319

Chain	Residue
A	LYS89
A	GLU150
A	TYR189
A	PRO225
A	ARG293
A	TRP295

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DMF A 320

Chain	Residue
A	TYR189
A	GLY213
A	ARG217
A	PRO225
A	SER226
A	LEU227
A	TRP295
A	HOH424

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DMF A 321

Chain	Residue
A	HIS46
A	THR81
A	TYR82
A	GLY118
A	LYS119
A	GLU120
A	PHE121

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE DMF A 322

Chain	Residue
A	TRP20
A	VAL47
A	TYR48
A	GLN49
A	NTI317
A	DMF332
A	DMF340
A	HOH430
A	HOH570

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMF A 323

Chain	Residue
A	GLY151
A	LYS154
A	ARG232
A	HOH607

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMF A 324

Chain	Residue
A	ILE196
A	GLN200
A	ARG255
A	HOH394

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMF A 325

Chain	Residue
A	GLN197
A	TYR198
A	HOH509

site_id	BC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMF A 326

Chain	Residue
A	ASP139
A	PRO173

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMF A 327

Chain	Residue
A	ASN8
A	GLY9
A	LYS154

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMF A 328

Chain	Residue
A	ASN7
A	ASN8
A	ALA155
A	ILE156
A	LYS178

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DMF A 329

Chain	Residue
A	PHE122
A	LEU124
A	SER302
A	NTI317
A	DMF331
A	DMF337
A	HOH486

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMF A 330

Chain	Residue
A	VAL148
A	ASP149
A	TYR177
A	SER290
A	HOH493

site_id	BC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMF A 331

Chain	Residue
A	NTI317
A	DMF329

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMF A 332

Chain	Residue
A	VAL47
A	PHE121
A	PHE122
A	NTI317
A	DMF322
A	HOH596

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMF A 333

Chain	Residue
A	DMF336
A	HOH446

site_id	CC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMF A 334

Chain	Residue
A	LEU175
A	LYS176
A	LYS178

site_id	CC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMF A 335

Chain	Residue
A	GLN59
A	GLU60
A	ARG63
A	HOH598

site_id	CC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMF A 336

Chain	Residue
A	LYS100
A	LEU101
A	ASP102
A	DMF333
A	HOH412
A	HOH446

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMF A 337

Chain	Residue
A	TRP219
A	CYS298
A	ALA299
A	LEU300
A	NTI317
A	DMF329

site_id	CC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMF A 338

Chain	Residue
A	ALA299
A	TYR309
A	PHE311

site_id	CC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMF A 339

Chain	Residue
A	TRP295
A	ARG296

site_id	CC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMF A 340

Chain	Residue
A	LYS21
A	PRO23
A	PRO24
A	TYR48
A	DMF322

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	MET144-PHE161

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

Chain	Residue	Details
A	ILE260-VAL275

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

Chain	Residue	Details
A	GLY38-GLY55

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"15272156","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	62
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15146478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15272156","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16337231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17368668","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17418233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17505104","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Site: {"description":"Lowers pKa of active site Tyr"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"8281941","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07943","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	3
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 725

Chain	Residue	Details
A	ASP43	electrostatic stabiliser
A	TYR48	proton acceptor, proton donor
A	LYS77	electrostatic stabiliser, modifies pKa
A	HIS110	electrostatic stabiliser

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