6MNC

CRYSTAL STRUCTURE OF HUMAN 17BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 1 COMPLEXED WITH ESTRONE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004303	molecular_function	estradiol 17-beta-dehydrogenase [NAD(P)+] activity
A	0005496	molecular_function	steroid binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006694	biological_process	steroid biosynthetic process
A	0006703	biological_process	estrogen biosynthetic process
A	0007040	biological_process	lysosome organization
A	0007519	biological_process	skeletal muscle tissue development
A	0008210	biological_process	estrogen metabolic process
A	0010467	biological_process	gene expression
A	0016491	molecular_function	oxidoreductase activity
A	0030283	molecular_function	testosterone dehydrogenase [NAD(P)+] activity
A	0036094	molecular_function	small molecule binding
A	0042803	molecular_function	protein homodimerization activity
A	0047035	molecular_function	testosterone dehydrogenase (NAD+) activity
A	0047045	molecular_function	testosterone 17-beta-dehydrogenase (NADP+) activity
A	0050661	molecular_function	NADP binding
A	0060348	biological_process	bone development
A	0060612	biological_process	adipose tissue development
A	0061370	biological_process	testosterone biosynthetic process
A	0070401	molecular_function	NADP+ binding
A	0071248	biological_process	cellular response to metal ion
A	0072582	molecular_function	17-beta-hydroxysteroid dehydrogenase (NADP+) activity
A	1903924	molecular_function	estradiol binding
B	0003824	molecular_function	catalytic activity
B	0004303	molecular_function	estradiol 17-beta-dehydrogenase [NAD(P)+] activity
B	0005496	molecular_function	steroid binding
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006694	biological_process	steroid biosynthetic process
B	0006703	biological_process	estrogen biosynthetic process
B	0007040	biological_process	lysosome organization
B	0007519	biological_process	skeletal muscle tissue development
B	0008210	biological_process	estrogen metabolic process
B	0010467	biological_process	gene expression
B	0016491	molecular_function	oxidoreductase activity
B	0030283	molecular_function	testosterone dehydrogenase [NAD(P)+] activity
B	0036094	molecular_function	small molecule binding
B	0042803	molecular_function	protein homodimerization activity
B	0047035	molecular_function	testosterone dehydrogenase (NAD+) activity
B	0047045	molecular_function	testosterone 17-beta-dehydrogenase (NADP+) activity
B	0050661	molecular_function	NADP binding
B	0060348	biological_process	bone development
B	0060612	biological_process	adipose tissue development
B	0061370	biological_process	testosterone biosynthetic process
B	0070401	molecular_function	NADP+ binding
B	0071248	biological_process	cellular response to metal ion
B	0072582	molecular_function	17-beta-hydroxysteroid dehydrogenase (NADP+) activity
B	1903924	molecular_function	estradiol binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue PEG A 401

Chain	Residue
A	GLY145
A	LEU146
A	PHE160
A	GLU163
A	ARG252
B	GLY145
B	ARG266

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site_id	AC2
Number of Residues	7
Details	binding site for residue J3Z B 401

Chain	Residue
B	PRO187
B	TYR218
B	HIS221
B	PHE259
B	GLU282
B	VAL143
B	TYR155

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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. SvgglmglpfNdvYCASKFALeGLCeSLA

Chain	Residue	Details
A	SER142-ALA170

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	TYR155
B	TYR155

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:8805577

Chain	Residue	Details
A	GLY9
A	ASP65
A	SER142
A	LYS159
B	GLY9
B	ASP65
B	SER142
B	LYS159

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:8994190

Chain	Residue	Details
A	SER134
B	SER134

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