6Y1P

Human Aldose Reductase Mutant L300/301A in Complex with a Ligand with an IDD Structure (3-({[2-(carboxymethoxy)-4-fluorobenzoyl]amino}methyl)benzoic acid)

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	0005739	cellular_component	mitochondrion
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	13
Details	binding site for residue 4G7 A 401

Chain	Residue
A	TRP20
A	CYS303
A	TYR309
A	NAP404
A	HOH520
A	VAL47
A	TYR48
A	TRP79
A	HIS110
A	TRP111
A	THR113
A	PHE122
A	ALA300

---

site_id	AC2
Number of Residues	8
Details	binding site for residue 4G7 A 402

Chain	Residue
A	TRP219
A	ARG296
A	VAL297
A	ALA299
A	ALA300
A	ALA301
A	HOH599
A	HOH632

---

site_id	AC3
Number of Residues	12
Details	binding site for residue CIT A 403

Chain	Residue
A	GLN49
A	ASN50
A	GLU51
A	ASN52
A	GLU53
A	LYS94
A	ASP98
A	HOH512
A	HOH671
A	HOH704
A	HOH708
A	HOH755

---

site_id	AC4
Number of Residues	37
Details	binding site for residue NAP A 404

Chain	Residue
A	GLY18
A	THR19
A	TRP20
A	LYS21
A	ASP43
A	TYR48
A	LYS77
A	HIS110
A	TRP111
A	SER159
A	ASN160
A	GLN183
A	TYR209
A	SER210
A	PRO211
A	LEU212
A	GLY213
A	SER214
A	PRO215
A	ASP216
A	LEU228
A	ALA245
A	ILE260
A	PRO261
A	LYS262
A	SER263
A	VAL264
A	THR265
A	ARG268
A	GLU271
A	ASN272
A	4G7401
A	HOH514
A	HOH556
A	HOH635
A	HOH668
A	HOH735

---

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	ACT_SITE: Proton donor => ECO:0000269|PubMed:15272156

Chain	Residue	Details
A	TYR48

---

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

Chain	Residue	Details
A	GLY9

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	HIS110

---

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	SER210

---

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

Chain	Residue	Details
A	LYS77

---

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	ALA1

---

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

Chain	Residue	Details
A	SER2

---

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

Chain	Residue	Details
A	LYS94
A	LYS221
A	LYS262

---

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

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