5LIY

Crystal structure of human AKR1B10 complexed with NADP+ and the inhibitor MK204

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0001523	biological_process	retinoid metabolic process
X	0001758	molecular_function	retinal dehydrogenase (NAD+) activity
X	0004032	molecular_function	aldose reductase (NADPH) activity
X	0005515	molecular_function	protein binding
X	0005576	cellular_component	extracellular region
X	0005739	cellular_component	mitochondrion
X	0005764	cellular_component	lysosome
X	0005829	cellular_component	cytosol
X	0006629	biological_process	lipid metabolic process
X	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
X	0016488	biological_process	farnesol catabolic process
X	0016491	molecular_function	oxidoreductase activity
X	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
X	0042572	biological_process	retinol metabolic process
X	0044597	biological_process	daunorubicin metabolic process
X	0044598	biological_process	doxorubicin metabolic process
X	0045550	molecular_function	geranylgeranyl reductase activity
X	0047655	molecular_function	allyl-alcohol dehydrogenase activity
X	0047718	molecular_function	indanol dehydrogenase activity
X	0052650	molecular_function	all-trans-retinol dehydrogenase (NADP+) activity
X	0110095	biological_process	cellular detoxification of aldehyde

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	binding site for residue NAP X 401

Chain	Residue
X	GLY19
X	TYR210
X	SER211
X	PRO212
X	LEU213
X	GLY214
X	SER215
X	PRO216
X	ASP217
X	ALA246
X	ILE261
X	THR20
X	PRO262
X	MLY263
X	SER264
X	VAL265
X	THR266
X	ARG269
X	GLU272
X	ASN273
X	DQP402
X	HOH520
X	TRP21
X	HOH527
X	ASP44
X	TYR49
X	HIS111
X	SER160
X	ASN161
X	GLN184

---

site_id	AC2
Number of Residues	16
Details	binding site for residue DQP X 402

Chain	Residue
X	TRP21
X	TYR49
X	TRP80
X	HIS111
X	TRP112
X	PHE123
X	TYR210
X	PRO219
X	TRP220
X	PRO232
X	CYS299
X	ASN300
X	LEU301
X	SER304
X	PHE312
X	NAP401

---

site_id	AC3
Number of Residues	4
Details	binding site for residue EDO X 403

Chain	Residue
X	GLU6
X	HIS201
X	THR206
X	ASN257

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
X	MET145-PHE162

---

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

Chain	Residue	Details
X	ILE261-VAL276

---

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

Chain	Residue	Details
X	GLY39-GLY56

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"18087047","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	13
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18087047","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Site: {"description":"Lowers pKa of active site Tyr","evidences":[{"source":"UniProtKB","id":"P14550","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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