2I17

Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 60K

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001523	biological_process	retinoid metabolic process
A	0001758	molecular_function	retinal dehydrogenase activity
A	0002070	biological_process	epithelial cell maturation
A	0003091	biological_process	renal water homeostasis
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	0005829	cellular_component	cytosol
A	0005975	biological_process	carbohydrate 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	0019853	biological_process	L-ascorbic acid biosynthetic process
A	0035809	biological_process	regulation of urine volume
A	0036130	molecular_function	prostaglandin H2 endoperoxidase reductase activity
A	0042572	biological_process	retinol metabolic process
A	0043066	biological_process	negative regulation of apoptotic 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
A	0072205	biological_process	metanephric collecting duct development

Functional Information from PDB Data

site_id	AC1
Number of Residues	39
Details	BINDING SITE FOR RESIDUE NDP A 319

Chain	Residue
A	GLY19
A	SER160
A	ASN161
A	GLN184
A	TYR210
A	SER211
A	PRO212
A	LEU213
A	GLY214
A	SER215
A	PRO216
A	THR20
A	ASP217
A	ALA246
A	ILE261
A	PRO262
A	LYS263
A	SER264
A	VAL265
A	THR266
A	ARG269
A	GLU272
A	TRP21
A	ASN273
A	LDT321
A	HOH572
A	HOH602
A	HOH603
A	HOH636
A	HOH875
A	HOH990
A	HOH991
A	HOH992
A	LYS22
A	ASP44
A	TYR49
A	LYS78
A	HIS111
A	TRP112

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE LDT A 321

Chain	Residue
A	TRP21
A	VAL48
A	TYR49
A	HIS111
A	TRP112
A	THR114
A	CYS299
A	ALA300
A	LEU301
A	NDP319

---

site_id	AC3
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CIT A 401

Chain	Residue
A	ASN163
A	HIS164
A	LYS195
A	LEU196
A	HOH452
A	HOH453
A	HOH454
A	HOH468
A	HOH469
A	HOH566
A	HOH568
A	HOH728
A	HOH760
A	HOH1031
A	HOH1039

---

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE CIT A 451

Chain	Residue
A	GLN50
A	ASN51
A	GLU52
A	ASN53
A	GLU54
A	LYS95
A	ASP99
A	HOH455
A	HOH456
A	HOH457
A	HOH458
A	HOH461
A	HOH462
A	HOH483
A	HOH492
A	HOH1040
A	HOH1041

---

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	MET145-PHE162

---

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

Chain	Residue	Details
A	ILE261-VAL276

---

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

Chain	Residue	Details
A	GLY39-GLY56

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:15272156

Chain	Residue	Details
A	GLN50

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	ALA11

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	TRP112

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:15146478, ECO:0000269|PubMed:15272156, ECO:0000269|PubMed:16337231, ECO:0000269|PubMed:17368668, ECO:0000269|PubMed:17418233, ECO:0000269|PubMed:17505104

Chain	Residue	Details
A	PRO212

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Lowers pKa of active site Tyr

Chain	Residue	Details
A	LEU79

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000269|PubMed:8281941, ECO:0007744|PubMed:19413330

Chain	Residue	Details
A	SER3

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07943

Chain	Residue	Details
A	ARG4

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	THR96
A	PRO223
A	SER264

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1mrq

Chain	Residue	Details
A	ASP44
A	HIS111
A	TYR49
A	LYS78

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1mrq

Chain	Residue	Details
A	TYR49
A	LYS78

---

site_id	MCSA1
Number of Residues	4
Details	M-CSA 725

Chain	Residue	Details
A	CYS45	electrostatic stabiliser
A	GLN50	proton acceptor, proton donor
A	LEU79	electrostatic stabiliser, modifies pKa
A	TRP112	electrostatic stabiliser

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