3BHI

Crystal structure of human Carbonyl Reductase 1 in complex with NADP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004090	molecular_function	carbonyl reductase (NADPH) activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006805	biological_process	xenobiotic metabolic process
A	0008106	molecular_function	alcohol dehydrogenase (NADP+) activity
A	0008211	biological_process	glucocorticoid metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0016655	molecular_function	oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
A	0019371	biological_process	cyclooxygenase pathway
A	0030855	biological_process	epithelial cell differentiation
A	0042373	biological_process	vitamin K metabolic process
A	0047020	molecular_function	15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity
A	0047021	molecular_function	15-hydroxyprostaglandin dehydrogenase (NADP+) activity
A	0050221	molecular_function	prostaglandin-E2 9-reductase activity
A	0070062	cellular_component	extracellular exosome
A	0160163	molecular_function	S-nitrosoglutathione reductase (NADPH) activity
A	1903561	cellular_component	extracellular vesicle
A	2000379	biological_process	positive regulation of reactive oxygen species metabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 308

Chain	Residue
A	ILE140
A	CYS226
A	PRO227
A	GLY228

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site_id	AC2
Number of Residues	33
Details	BINDING SITE FOR RESIDUE NAP A 309

Chain	Residue
A	ARG37
A	ARG41
A	LEU61
A	ASP62
A	ILE63
A	ASP64
A	ASN89
A	ALA90
A	GLY91
A	SER138
A	TYR193
A	LYS197
A	PRO227
A	GLY228
A	TRP229
A	THR232
A	ASP233
A	MET234
A	HOH311
A	HOH312
A	HOH316
A	HOH334
A	HOH337
A	HOH339
A	HOH404
A	HOH415
A	HOH416
A	HOH454
A	GLY11
A	ASN13
A	LYS14
A	GLY15
A	ILE16

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Functional Information from PROSITE/UniProt

site_id	PS00061
Number of Residues	29
Details	ADH_SHORT Short-chain dehydrogenases/reductases family signature. KgvhqkegwpSsaYGVTKIGVtVLSrIHA

Chain	Residue	Details
A	LYS180-ALA208

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	TYR193

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING: BINDING => ECO:0000269|PubMed:15799708, ECO:0000269|PubMed:17912391, ECO:0000269|PubMed:18826943

Chain	Residue	Details
A	VAL9
A	ASP62
A	ASN89
A	TYR193
A	VAL230

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING:

Chain	Residue	Details
A	PHE94
A	GLN105
A	SER139
A	ALA192

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47727

Chain	Residue	Details
A	SER1

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48758

Chain	Residue	Details
A	SER29

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-1-carboxyethyl lysine => ECO:0000269|PubMed:8421682

Chain	Residue	Details
A	LYS238

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1db3

Chain	Residue	Details
A	GLU152
A	TYR193
A	SER139
A	LYS197

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1db3

Chain	Residue	Details
A	ASN113
A	TYR193
A	SER139
A	LYS197

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1db3

Chain	Residue	Details
A	LYS197
A	SER190

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site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1db3

Chain	Residue	Details
A	TYR193
A	LYS197

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