2QXW

Perdeuterated alr2 in complex with idd594

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	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	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 318

Chain	Residue
A	GLY18
A	SER159
A	ASN160
A	GLN183
A	TYR209
A	SER210
A	PRO211
A	LEU212
A	GLY213
A	SER214
A	PRO215
A	THR19
A	ASP216
A	ALA245
A	ILE260
A	PRO261
A	LYS262
A	SER263
A	VAL264
A	THR265
A	ARG268
A	GLU271
A	TRP20
A	ASN272
A	LDT320
A	HOH641
A	HOH682
A	HOH685
A	HOH2233
A	HOH2633
A	HOH4504
A	HOH4505
A	HOH4506
A	LYS21
A	ASP43
A	TYR48
A	LYS77
A	HIS110
A	TRP111

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE LDT A 320

Chain	Residue
A	TRP20
A	VAL47
A	TYR48
A	HIS110
A	TRP111
A	THR113
A	PHE122
A	CYS298
A	ALA299
A	LEU300
A	NDP318

---

site_id	AC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CIT A 400

Chain	Residue
A	ASN162
A	HIS163
A	LYS194
A	LEU195
A	HOH411
A	HOH412
A	HOH415
A	HOH506
A	HOH507
A	HOH632
A	HOH637
A	HOH2365
A	HOH2411

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CIT A 450

Chain	Residue
A	GLN49
A	ASN50
A	GLU51
A	ASN52
A	GLU53
A	LYS94
A	ASP98
A	HOH460
A	HOH461
A	HOH462
A	HOH463
A	HOH466
A	HOH471
A	HOH527
A	HOH542

---

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

Chain	Residue	Details
A	TYR48
A	ASP43
A	HIS110
A	LYS77

---

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

Chain	Residue	Details
A	TYR48
A	LYS77

---

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

---