5EPO

The three-dimensional structure of Clostridium absonum 7alpha-hydroxysteroid dehydrogenase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0016042	biological_process	lipid catabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0030573	biological_process	bile acid catabolic process
B	0000166	molecular_function	nucleotide binding
B	0016042	biological_process	lipid catabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0030573	biological_process	bile acid catabolic process
C	0000166	molecular_function	nucleotide binding
C	0016042	biological_process	lipid catabolic process
C	0016491	molecular_function	oxidoreductase activity
C	0030573	biological_process	bile acid catabolic process
D	0000166	molecular_function	nucleotide binding
D	0016042	biological_process	lipid catabolic process
D	0016491	molecular_function	oxidoreductase activity
D	0030573	biological_process	bile acid catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	binding site for residue NAP A 301

Chain	Residue
A	SER13
A	ASN90
A	TYR91
A	GLY92
A	ILE143
A	TYR158
A	LYS162
A	PRO188
A	GLY189
A	ILE191
A	THR193
A	THR15
A	ARG194
A	ALA195
A	ALA196
A	TUD302
A	HOH407
A	HOH423
A	HOH427
A	HOH435
A	HOH446
A	HOH458
A	ARG16
A	HOH528
A	GLY17
A	ILE18
A	ARG38
A	PHE62
A	ASN63
A	ALA64

---

site_id	AC2
Number of Residues	14
Details	binding site for residue TUD A 302

Chain	Residue
A	GLY93
A	THR94
A	THR145
A	GLY147
A	ARG155
A	TYR158
A	GLY189
A	ALA196
A	ASN199
A	PHE204
A	NAP301
A	HOH421
A	HOH443
A	HOH476

---

site_id	AC3
Number of Residues	9
Details	binding site for residue GOL A 303

Chain	Residue
A	LYS7
A	GLY138
A	ARG182
A	ALA231
A	SER232
A	ASP233
A	HOH418
A	HOH501
A	HOH563

---

site_id	AC4
Number of Residues	32
Details	binding site for residue NAP B 301

Chain	Residue
B	SER13
B	THR15
B	ARG16
B	GLY17
B	ILE18
B	ARG38
B	LEU42
B	PHE62
B	ASN63
B	ALA64
B	ASN90
B	TYR91
B	GLY92
B	ILE143
B	TYR158
B	LYS162
B	PRO188
B	GLY189
B	ILE191
B	THR193
B	ARG194
B	ALA195
B	ALA196
B	TUD302
B	HOH401
B	HOH416
B	HOH423
B	HOH437
B	HOH451
B	HOH464
B	HOH478
B	HOH511

---

site_id	AC5
Number of Residues	13
Details	binding site for residue TUD B 302

Chain	Residue
B	GLY93
B	THR94
B	THR145
B	GLY147
B	ARG155
B	TYR158
B	GLY189
B	ALA196
B	ASN199
B	PHE204
B	NAP301
B	HOH424
B	HOH518

---

site_id	AC6
Number of Residues	10
Details	binding site for residue GOL B 303

Chain	Residue
B	GLY138
B	ARG182
B	ALA231
B	SER232
B	ASP233
B	HOH408
B	HOH446
B	HOH472
B	HOH485
B	LYS7

---

site_id	AC7
Number of Residues	32
Details	binding site for residue NAP C 301

Chain	Residue
C	SER13
C	THR15
C	ARG16
C	GLY17
C	ILE18
C	ARG38
C	PHE62
C	ASN63
C	ALA64
C	ASN90
C	TYR91
C	GLY92
C	SER144
C	TYR158
C	LYS162
C	PRO188
C	GLY189
C	ILE191
C	THR193
C	ARG194
C	ALA195
C	ALA196
C	TUD302
C	HOH431
C	HOH450
C	HOH465
C	HOH470
C	HOH492
C	HOH503
C	HOH528
C	HOH531
C	HOH565

---

site_id	AC8
Number of Residues	14
Details	binding site for residue TUD C 302

Chain	Residue
C	GLY93
C	THR94
C	VAL96
C	THR145
C	GLY147
C	ARG155
C	TYR158
C	GLY189
C	ALA196
C	ASN199
C	NAP301
C	HOH441
C	HOH486
C	HOH521

---

site_id	AC9
Number of Residues	9
Details	binding site for residue GOL C 303

Chain	Residue
C	LYS7
C	GLY138
C	ARG182
C	ALA231
C	SER232
C	ASP233
C	HOH417
C	HOH483
C	HOH501

---

site_id	AD1
Number of Residues	30
Details	binding site for residue NAP D 301

Chain	Residue
D	SER13
D	THR15
D	ARG16
D	GLY17
D	ILE18
D	ARG38
D	PHE62
D	ASN63
D	ALA64
D	ASN90
D	TYR91
D	GLY92
D	SER144
D	TYR158
D	LYS162
D	GLY189
D	ILE191
D	THR193
D	ARG194
D	ALA195
D	ALA196
D	TUD302
D	HOH407
D	HOH418
D	HOH472
D	HOH505
D	HOH508
D	HOH523
D	HOH529
D	HOH536

---

site_id	AD2
Number of Residues	16
Details	binding site for residue TUD D 302

Chain	Residue
D	GLY93
D	THR94
D	ASN95
D	VAL96
D	THR145
D	GLY147
D	TYR158
D	GLY189
D	ALA196
D	ASN199
D	MET200
D	PHE204
D	NAP301
D	HOH434
D	HOH449
D	HOH504

---

site_id	AD3
Number of Residues	10
Details	binding site for residue GOL D 303

Chain	Residue
D	ILE86
D	GLY138
D	ARG182
D	ALA231
D	ASP233
D	HOH401
D	HOH428
D	HOH446
D	HOH450
D	HOH518

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P0AET8

Chain	Residue	Details
A	TYR158
B	TYR158
C	TYR158
D	TYR158

---

site_id	SWS_FT_FI2
Number of Residues	32
Details	BINDING: BINDING => ECO:0000269|PubMed:26961171, ECO:0007744|PDB:5EPO

Chain	Residue	Details
A	SER13
B	ARG38
B	ASN63
B	ASN90
B	THR145
B	TYR158
B	LYS162
B	ILE191
C	SER13
C	ARG38
C	ASN63
A	ARG38
C	ASN90
C	THR145
C	TYR158
C	LYS162
C	ILE191
D	SER13
D	ARG38
D	ASN63
D	ASN90
D	THR145
A	ASN63
D	TYR158
D	LYS162
D	ILE191
A	ASN90
A	THR145
A	TYR158
A	LYS162
A	ILE191
B	SER13

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	SITE: Lowers pKa of active site Tyr => ECO:0000250|UniProtKB:P0AET8

Chain	Residue	Details
A	LYS162
B	LYS162
C	LYS162
D	LYS162

---