Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1FDU

HUMAN 17-BETA-HYDROXYSTEROID-DEHYDROGENASE TYPE 1 MUTANT H221L COMPLEXED WITH ESTRADIOL AND NADP+

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0016491	molecular_function	oxidoreductase 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 dehydrogenase (NADP+) activity
A	0050661	molecular_function	NADP binding
A	0060348	biological_process	bone 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	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	0016491	molecular_function	oxidoreductase 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 dehydrogenase (NADP+) activity
B	0050661	molecular_function	NADP binding
B	0060348	biological_process	bone 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
C	0004303	molecular_function	estradiol 17-beta-dehydrogenase [NAD(P)+] activity
C	0005496	molecular_function	steroid binding
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006629	biological_process	lipid metabolic process
C	0006694	biological_process	steroid biosynthetic process
C	0006703	biological_process	estrogen biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0036094	molecular_function	small molecule binding
C	0042803	molecular_function	protein homodimerization activity
C	0047035	molecular_function	testosterone dehydrogenase (NAD+) activity
C	0047045	molecular_function	testosterone dehydrogenase (NADP+) activity
C	0050661	molecular_function	NADP binding
C	0060348	biological_process	bone development
C	0061370	biological_process	testosterone biosynthetic process
C	0070401	molecular_function	NADP+ binding
C	0071248	biological_process	cellular response to metal ion
C	0072582	molecular_function	17-beta-hydroxysteroid dehydrogenase (NADP+) activity
C	1903924	molecular_function	estradiol binding
D	0004303	molecular_function	estradiol 17-beta-dehydrogenase [NAD(P)+] activity
D	0005496	molecular_function	steroid binding
D	0005515	molecular_function	protein binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006629	biological_process	lipid metabolic process
D	0006694	biological_process	steroid biosynthetic process
D	0006703	biological_process	estrogen biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0036094	molecular_function	small molecule binding
D	0042803	molecular_function	protein homodimerization activity
D	0047035	molecular_function	testosterone dehydrogenase (NAD+) activity
D	0047045	molecular_function	testosterone dehydrogenase (NADP+) activity
D	0050661	molecular_function	NADP binding
D	0060348	biological_process	bone development
D	0061370	biological_process	testosterone biosynthetic process
D	0070401	molecular_function	NADP+ binding
D	0071248	biological_process	cellular response to metal ion
D	0072582	molecular_function	17-beta-hydroxysteroid dehydrogenase (NADP+) activity
D	1903924	molecular_function	estradiol binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	SER12
A	GLY13
A	HIS17
A	THR190

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 B 400

Chain	Residue
B	HIS17
B	ARG44
B	PRO233
B	SER12
B	GLY13

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 C 403

Chain	Residue
C	SER12
C	GLY13
C	HIS17
C	ARG44
C	THR190
C	HOH660

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SO4 D 402

Chain	Residue
D	SER12
D	GLY13
D	HIS17
D	ARG44
D	HIS189
D	THR190
D	PRO233

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE EST A 351

Chain	Residue
A	SER142
A	VAL143
A	GLY144
A	LEU149
A	TYR155
A	PRO187
A	PHE192
A	TYR218
A	SER222
A	NAP361

site_id	AC6
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAP A 361

Chain	Residue
A	GLY9
A	SER11
A	SER12
A	GLY13
A	ILE14
A	ARG37
A	LEU64
A	ASP65
A	VAL66
A	ARG67
A	ASN90
A	ALA91
A	GLY92
A	VAL113
A	THR140
A	GLY141
A	SER142
A	TYR155
A	LYS159
A	CYS185
A	GLY186
A	PRO187
A	VAL188
A	THR190
A	ALA191
A	PHE192
A	LYS195
A	PHE226
A	EST351
A	HOH508
A	HOH524
A	HOH565
A	HOH630
A	HOH673

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EST B 354

Chain	Residue
B	SER142
B	VAL143
B	GLY144
B	LEU149
B	TYR155
B	PHE226
B	PHE259
B	MET279
B	NAP364

site_id	AC8
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAP B 364

Chain	Residue
B	ALA191
B	PHE192
B	LYS195
B	PHE226
B	EST354
B	HOH551
B	HOH554
B	HOH614
B	HOH641
B	HOH645
B	GLY9
B	SER11
B	SER12
B	GLY13
B	ILE14
B	ARG37
B	LEU64
B	ASP65
B	VAL66
B	ARG67
B	ASN90
B	ALA91
B	THR140
B	GLY141
B	SER142
B	LYS159
B	CYS185
B	GLY186
B	PRO187
B	VAL188
B	THR190

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE EST C 353

Chain	Residue
C	SER142
C	VAL143
C	GLY144
C	LEU149
C	TYR155
C	PRO187
C	TYR218
C	SER222
C	PHE259
C	MET279
C	VAL283
C	NAP363

site_id	BC1
Number of Residues	31
Details	BINDING SITE FOR RESIDUE NAP C 363

Chain	Residue
C	GLY9
C	SER11
C	SER12
C	GLY13
C	ILE14
C	ARG37
C	LEU64
C	ASP65
C	VAL66
C	ARG67
C	ASN90
C	ALA91
C	GLY92
C	VAL113
C	THR140
C	GLY141
C	SER142
C	TYR155
C	LYS159
C	CYS185
C	GLY186
C	PRO187
C	VAL188
C	THR190
C	PHE192
C	LYS195
C	PHE226
C	EST353
C	HOH509
C	HOH575
C	HOH678

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EST D 352

Chain	Residue
D	SER142
D	VAL143
D	GLY144
D	LEU149
D	TYR155
D	PHE259
D	NAP362

site_id	BC3
Number of Residues	29
Details	BINDING SITE FOR RESIDUE NAP D 362

Chain	Residue
D	GLY9
D	SER11
D	SER12
D	GLY13
D	ILE14
D	ARG37
D	LEU64
D	ASP65
D	VAL66
D	ASN90
D	ALA91
D	GLY92
D	THR140
D	GLY141
D	SER142
D	LYS159
D	CYS185
D	GLY186
D	PRO187
D	VAL188
D	THR190
D	ALA191
D	PHE192
D	LYS195
D	PHE226
D	EST352
D	HOH530
D	HOH590
D	HOH639

site_id	CAT
Number of Residues	3
Details	CATALYTIC SITE.

Chain	Residue
A	SER142
A	TYR155
A	LYS159

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	124
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8805577","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"8994190","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	ASN152
A	LYS159

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	ASN152
B	LYS159

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

Chain	Residue	Details
C	ASN152
C	LYS159

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

Chain	Residue	Details
D	ASN152
D	LYS159

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
A	TYR155
A	LYS159

site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
B	TYR155
B	LYS159

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
C	TYR155
C	LYS159

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1qsg

Chain	Residue	Details
D	TYR155
D	LYS159

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)