3BHM

Crystal structure of human Carbonyl Reductase 1 in complex with S-hydroxymethylglutathione

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	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	3
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	ARG57
A	PHE58
A	HOH522

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 402

Chain	Residue
A	LYS14
A	GLY15
A	HOH408
A	HOH432

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 403

Chain	Residue
A	HOH599
A	ARG118
A	HOH539

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 404

Chain	Residue
A	LYS216
A	GLY217
A	ASP218
A	LYS219
A	HOH479

---

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AHE A 304

Chain	Residue
A	ALA93
A	PHE94
A	LYS95
A	PHE102
A	GLN105
A	SER190
A	SER191
A	ALA192
A	TYR193
A	MET234
A	HOH416
A	HOH459
A	HOH521
A	HOH603

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE AB3 A 307

Chain	Residue
A	LEU27
A	SER139
A	TYR193
A	GLY228
A	TRP229
A	HOH561
A	HOH603

---

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE AB3 A 308

Chain	Residue
A	ARG22
A	ARG26
A	ILE140
A	ARG144
A	GLU244

---

site_id	AC8
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAP A 309

Chain	Residue
A	GLY11
A	ASN13
A	LYS14
A	GLY15
A	ILE16
A	ARG37
A	LEU61
A	ASP62
A	ILE63
A	ASP64
A	ASN89
A	ALA90
A	GLY91
A	ILE92
A	SER138
A	TYR193
A	LYS197
A	PRO227
A	GLY228
A	TRP229
A	THR232
A	ASP233
A	MET234
A	ALA235
A	HOH406
A	HOH410
A	HOH413
A	HOH431
A	HOH432
A	HOH470
A	HOH477
A	HOH481
A	HOH512
A	HOH590

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	TYR193

---

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

---