3KLP

17beta-HSD1 in complex with A-diol

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE B81 X 328

Chain	Residue
X	TYR218
X	HIS221
X	SER222
X	PHE259
X	MET279
X	GLU282
X	VAL283

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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
X	SER142-ALA170

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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
X	TYR155

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:8805577

Chain	Residue	Details
X	GLY9
X	ASP65
X	SER142
X	LYS159

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:8994190

Chain	Residue	Details
X	SER134

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