Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4IS3

Crystal structure of a 3alpha-hydroxysteroid dehydrogenase (BaiA2) associated with secondary bile acid synthesis from Clostridium scindens VPI12708 in complex with a putative NAD(+)-OH- adduct at 2.0 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006629	biological_process	lipid metabolic process
A	0008202	biological_process	steroid metabolic process
A	0008206	biological_process	bile acid 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	0030573	biological_process	bile acid catabolic process
A	0032052	molecular_function	bile acid binding
A	0033764	molecular_function	steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A	0033792	molecular_function	3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase activity
A	0051289	biological_process	protein homotetramerization
A	0070403	molecular_function	NAD+ binding
A	1903412	biological_process	response to bile acid
B	0005737	cellular_component	cytoplasm
B	0006629	biological_process	lipid metabolic process
B	0008202	biological_process	steroid metabolic process
B	0008206	biological_process	bile acid metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0030573	biological_process	bile acid catabolic process
B	0032052	molecular_function	bile acid binding
B	0033764	molecular_function	steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B	0033792	molecular_function	3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase activity
B	0051289	biological_process	protein homotetramerization
B	0070403	molecular_function	NAD+ binding
B	1903412	biological_process	response to bile acid
C	0005737	cellular_component	cytoplasm
C	0006629	biological_process	lipid metabolic process
C	0008202	biological_process	steroid metabolic process
C	0008206	biological_process	bile acid metabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0030573	biological_process	bile acid catabolic process
C	0032052	molecular_function	bile acid binding
C	0033764	molecular_function	steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C	0033792	molecular_function	3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase activity
C	0051289	biological_process	protein homotetramerization
C	0070403	molecular_function	NAD+ binding
C	1903412	biological_process	response to bile acid
D	0005737	cellular_component	cytoplasm
D	0006629	biological_process	lipid metabolic process
D	0008202	biological_process	steroid metabolic process
D	0008206	biological_process	bile acid metabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0016616	molecular_function	oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0030573	biological_process	bile acid catabolic process
D	0032052	molecular_function	bile acid binding
D	0033764	molecular_function	steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D	0033792	molecular_function	3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase activity
D	0051289	biological_process	protein homotetramerization
D	0070403	molecular_function	NAD+ binding
D	1903412	biological_process	response to bile acid

Functional Information from PDB Data

site_id	AC1
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NAD A 300

Chain	Residue
A	GLY13
A	ALA93
A	GLY94
A	ILE95
A	ILE115
A	THR142
A	ALA143
A	SER144
A	TYR157
A	LYS161
A	PRO187
A	THR15
A	GLY188
A	VAL189
A	VAL190
A	THR192
A	MSE194
A	THR195
A	HOH488
A	HOH523
A	HOH531
A	HOH669
A	ARG16
A	HOH676
A	HOH702
A	HOH716
A	HOH970
A	HOH975
A	HOH1069
A	GLY17
A	ILE18
A	GLU38
A	GLU42
A	LEU66
A	ASN92

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT A 400

Chain	Residue
A	THR15
A	ARG16
A	GLU42

site_id	AC3
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NAD B 300

Chain	Residue
B	GLY13
B	THR15
B	ARG16
B	GLY17
B	ILE18
B	GLU38
B	GLU42
B	LEU66
B	ASN92
B	ALA93
B	GLY94
B	ILE95
B	ILE115
B	THR142
B	ALA143
B	SER144
B	TYR157
B	LYS161
B	PRO187
B	GLY188
B	VAL189
B	VAL190
B	THR192
B	MSE194
B	THR195
B	HOH464
B	HOH540
B	HOH681
B	HOH738
B	HOH739
B	HOH764
B	HOH771
B	HOH912
B	HOH990
B	HOH993

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT B 401

Chain	Residue
B	THR15
B	ARG16
B	GLU42
B	HOH959

site_id	AC5
Number of Residues	35
Details	BINDING SITE FOR RESIDUE NAD C 300

Chain	Residue
C	THR192
C	ASP193
C	MSE194
C	THR195
C	HOH504
C	HOH506
C	HOH562
C	HOH682
C	HOH833
C	HOH916
C	HOH1008
C	HOH1009
C	HOH1023
C	GLY13
C	THR15
C	ARG16
C	GLY17
C	ILE18
C	GLU38
C	GLU42
C	LEU66
C	ASN92
C	ALA93
C	GLY94
C	ILE95
C	ILE115
C	THR142
C	ALA143
C	SER144
C	TYR157
C	LYS161
C	PRO187
C	GLY188
C	VAL189
C	VAL190

site_id	AC6
Number of Residues	34
Details	BINDING SITE FOR RESIDUE NAD D 300

Chain	Residue
D	GLY13
D	THR15
D	ARG16
D	GLY17
D	ILE18
D	GLU38
D	GLU42
D	LEU66
D	ASN92
D	ALA93
D	GLY94
D	ILE95
D	ILE115
D	THR142
D	ALA143
D	SER144
D	TYR157
D	LYS161
D	PRO187
D	GLY188
D	VAL189
D	VAL190
D	THR192
D	MSE194
D	THR195
D	HOH530
D	HOH838
D	HOH839
D	HOH841
D	HOH848
D	HOH961
D	HOH1025
D	HOH1124
D	HOH1125

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER144-GLY172

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10001","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23836456","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"23836456","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	36
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23836456","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4IS3","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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