Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PD6

Structure of human hydroxysteroid dehydrogenase type 8, HSD17B8

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004303	molecular_function	estradiol 17-beta-dehydrogenase [NAD(P)+] activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005740	cellular_component	mitochondrial envelope
A	0005759	cellular_component	mitochondrial matrix
A	0005783	cellular_component	endoplasmic reticulum
A	0005886	cellular_component	plasma membrane
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006694	biological_process	steroid biosynthetic process
A	0006703	biological_process	estrogen biosynthetic process
A	0008210	biological_process	estrogen metabolic process
A	0016020	cellular_component	membrane
A	0016491	molecular_function	oxidoreductase activity
A	0047035	molecular_function	testosterone dehydrogenase (NAD+) activity
A	0048038	molecular_function	quinone binding
A	0051290	biological_process	protein heterotetramerization
A	0070404	molecular_function	NADH binding
A	0106386	molecular_function	(3R)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
A	1990204	cellular_component	oxidoreductase complex
B	0004303	molecular_function	estradiol 17-beta-dehydrogenase [NAD(P)+] activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005740	cellular_component	mitochondrial envelope
B	0005759	cellular_component	mitochondrial matrix
B	0005783	cellular_component	endoplasmic reticulum
B	0005886	cellular_component	plasma membrane
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0006694	biological_process	steroid biosynthetic process
B	0006703	biological_process	estrogen biosynthetic process
B	0008210	biological_process	estrogen metabolic process
B	0016020	cellular_component	membrane
B	0016491	molecular_function	oxidoreductase activity
B	0047035	molecular_function	testosterone dehydrogenase (NAD+) activity
B	0048038	molecular_function	quinone binding
B	0051290	biological_process	protein heterotetramerization
B	0070404	molecular_function	NADH binding
B	0106386	molecular_function	(3R)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
B	1990204	cellular_component	oxidoreductase complex
C	0004303	molecular_function	estradiol 17-beta-dehydrogenase [NAD(P)+] activity
C	0005515	molecular_function	protein binding
C	0005739	cellular_component	mitochondrion
C	0005740	cellular_component	mitochondrial envelope
C	0005759	cellular_component	mitochondrial matrix
C	0005783	cellular_component	endoplasmic reticulum
C	0005886	cellular_component	plasma membrane
C	0006629	biological_process	lipid metabolic process
C	0006631	biological_process	fatty acid metabolic process
C	0006633	biological_process	fatty acid biosynthetic process
C	0006694	biological_process	steroid biosynthetic process
C	0006703	biological_process	estrogen biosynthetic process
C	0008210	biological_process	estrogen metabolic process
C	0016020	cellular_component	membrane
C	0016491	molecular_function	oxidoreductase activity
C	0047035	molecular_function	testosterone dehydrogenase (NAD+) activity
C	0048038	molecular_function	quinone binding
C	0051290	biological_process	protein heterotetramerization
C	0070404	molecular_function	NADH binding
C	0106386	molecular_function	(3R)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
C	1990204	cellular_component	oxidoreductase complex
D	0004303	molecular_function	estradiol 17-beta-dehydrogenase [NAD(P)+] activity
D	0005515	molecular_function	protein binding
D	0005739	cellular_component	mitochondrion
D	0005740	cellular_component	mitochondrial envelope
D	0005759	cellular_component	mitochondrial matrix
D	0005783	cellular_component	endoplasmic reticulum
D	0005886	cellular_component	plasma membrane
D	0006629	biological_process	lipid metabolic process
D	0006631	biological_process	fatty acid metabolic process
D	0006633	biological_process	fatty acid biosynthetic process
D	0006694	biological_process	steroid biosynthetic process
D	0006703	biological_process	estrogen biosynthetic process
D	0008210	biological_process	estrogen metabolic process
D	0016020	cellular_component	membrane
D	0016491	molecular_function	oxidoreductase activity
D	0047035	molecular_function	testosterone dehydrogenase (NAD+) activity
D	0048038	molecular_function	quinone binding
D	0051290	biological_process	protein heterotetramerization
D	0070404	molecular_function	NADH binding
D	0106386	molecular_function	(3R)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity
D	1990204	cellular_component	oxidoreductase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD A 1

Chain	Residue
A	GLY18
A	CYS103
A	ALA104
A	VAL126
A	ILE154
A	SER155
A	SER156
A	TYR169
A	LYS173
A	PRO199
A	GLY200
A	SER21
A	ILE202
A	THR204
A	PRO205
A	MET206
A	HOH278
A	HOH285
A	HOH337
A	GLY22
A	ILE23
A	ASP42
A	LEU43
A	ALA74
A	ASP75
A	VAL76

site_id	AC2
Number of Residues	24
Details	BINDING SITE FOR RESIDUE NAD B 2

Chain	Residue
B	GLY18
B	SER21
B	GLY22
B	ILE23
B	ASP42
B	LEU43
B	ALA74
B	ASP75
B	VAL76
B	CYS103
B	ALA104
B	GLY105
B	ILE154
B	SER155
B	SER156
B	TYR169
B	LYS173
B	PRO199
B	GLY200
B	ILE202
B	THR204
B	PRO205
B	MET206
B	THR207

site_id	AC3
Number of Residues	23
Details	BINDING SITE FOR RESIDUE NAD C 3

Chain	Residue
C	GLY18
C	SER21
C	GLY22
C	ILE23
C	ASP42
C	LEU43
C	ALA74
C	ASP75
C	VAL76
C	CYS103
C	ILE154
C	SER155
C	TYR169
C	LYS173
C	PRO199
C	GLY200
C	ILE202
C	THR204
C	PRO205
C	MET206
C	THR207
C	HOH288
C	HOH306

site_id	AC4
Number of Residues	26
Details	BINDING SITE FOR RESIDUE NAD D 4

Chain	Residue
D	GLY18
D	SER21
D	GLY22
D	ILE23
D	ASP42
D	LEU43
D	ALA74
D	ASP75
D	VAL76
D	CYS103
D	ALA104
D	GLY105
D	ILE154
D	SER155
D	SER156
D	TYR169
D	LYS173
D	PRO199
D	GLY200
D	ILE202
D	THR204
D	PRO205
D	MET206
D	THR207
D	HOH282
D	HOH291

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER156-ALA184

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25203508","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Structure of human hydroxysteroid dehydrogenase type 8, HSD17B8.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2PD6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CQL","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Structure of human hydroxysteroid dehydrogenase type 8, HSD17B8.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"2PD6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4CQM","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P50171","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

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

Chain	Residue	Details
A	SER156
A	TYR169
A	ASN127
A	LYS173

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
B	TYR169
B	LYS173

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
C	TYR169
C	LYS173

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
D	TYR169
D	LYS173

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

Chain	Residue	Details
B	SER156
B	TYR169
B	ASN127
B	LYS173

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
C	SER156
C	TYR169
C	ASN127
C	LYS173

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
D	SER156
D	TYR169
D	ASN127
D	LYS173

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

Chain	Residue	Details
A	GLN166
A	LYS173

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

Chain	Residue	Details
B	GLN166
B	LYS173

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

Chain	Residue	Details
C	GLN166
C	LYS173

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

Chain	Residue	Details
D	GLN166
D	LYS173

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1ybv

Chain	Residue	Details
A	TYR169
A	LYS173

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