Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4XGN

Crystal structure of 3-hydroxyacyl-CoA dehydrogenase in complex with NAD from Burkholderia thailandensis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0016491	molecular_function	oxidoreductase activity
B	0000166	molecular_function	nucleotide binding
B	0016491	molecular_function	oxidoreductase activity
C	0000166	molecular_function	nucleotide binding
C	0016491	molecular_function	oxidoreductase activity
D	0000166	molecular_function	nucleotide binding
D	0016491	molecular_function	oxidoreductase activity
E	0000166	molecular_function	nucleotide binding
E	0016491	molecular_function	oxidoreductase activity
F	0000166	molecular_function	nucleotide binding
F	0016491	molecular_function	oxidoreductase activity
G	0000166	molecular_function	nucleotide binding
G	0016491	molecular_function	oxidoreductase activity
H	0000166	molecular_function	nucleotide binding
H	0016491	molecular_function	oxidoreductase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	30
Details	binding site for residue NAD A 300

Chain	Residue
A	GLY12
A	CYS83
A	ALA84
A	THR143
A	ALA144
A	TYR158
A	LYS162
A	PRO188
A	GLY189
A	ILE190
A	PHE191
A	SER15
A	THR193
A	PRO194
A	MET195
A	EDO301
A	HOH460
A	HOH467
A	HOH469
A	HOH471
A	HOH506
A	HOH513
A	GLY16
A	HOH565
A	LEU17
A	ASP36
A	LEU37
A	CYS56
A	ASP57
A	VAL58

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 301

Chain	Residue
A	TYR158
A	NAD300
A	HOH466
A	HOH524

site_id	AC3
Number of Residues	5
Details	binding site for residue EDO A 302

Chain	Residue
A	MET210
A	ILE247
A	ARG248
A	MET249
A	GLN250

site_id	AC4
Number of Residues	32
Details	binding site for residue NAD B 300

Chain	Residue
B	GLY12
B	SER15
B	GLY16
B	LEU17
B	ASP36
B	LEU37
B	CYS56
B	ASP57
B	VAL58
B	CYS83
B	ALA84
B	GLY85
B	VAL110
B	THR143
B	ALA144
B	TYR158
B	LYS162
B	PRO188
B	GLY189
B	ILE190
B	PHE191
B	THR193
B	PRO194
B	MET195
B	EDO301
B	HOH447
B	HOH450
B	HOH461
B	HOH480
B	HOH507
B	HOH522
B	HOH527

site_id	AC5
Number of Residues	4
Details	binding site for residue EDO B 301

Chain	Residue
B	TYR158
B	NAD300
B	HOH479
B	HOH603

site_id	AC6
Number of Residues	4
Details	binding site for residue EDO B 302

Chain	Residue
B	ARG248
B	MET249
B	GLN250
B	HOH639

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

Chain	Residue
C	PHE191
C	THR193
C	PRO194
C	MET195
C	EDO302
C	HOH445
C	HOH467
C	HOH468
C	HOH505
C	HOH508
C	HOH517
C	HOH537
C	GLY12
C	SER15
C	GLY16
C	LEU17
C	ASP36
C	LEU37
C	CYS56
C	ASP57
C	VAL58
C	CYS83
C	ALA84
C	GLY85
C	VAL110
C	THR143
C	ALA144
C	TYR158
C	LYS162
C	PRO188
C	GLY189
C	ILE190

site_id	AC8
Number of Residues	4
Details	binding site for residue EDO C 302

Chain	Residue
C	TYR158
C	NAD301
C	HOH530
C	HOH602

site_id	AC9
Number of Residues	6
Details	binding site for residue GOL C 303

Chain	Residue
B	GLU239
B	VAL240
C	GLU239
C	VAL240
C	HOH435
C	HOH459

site_id	AD1
Number of Residues	8
Details	binding site for residue GOL D 301

Chain	Residue
A	GLU239
A	VAL240
A	ARG242
D	GLU239
D	VAL240
D	HOH437
D	HOH441
D	HOH595

site_id	AD2
Number of Residues	31
Details	binding site for residue NAD D 302

Chain	Residue
D	GLY12
D	SER15
D	GLY16
D	LEU17
D	ASP36
D	LEU37
D	CYS56
D	ASP57
D	VAL58
D	CYS83
D	ALA84
D	GLY85
D	THR143
D	ALA144
D	TYR158
D	LYS162
D	PRO188
D	GLY189
D	ILE190
D	PHE191
D	THR193
D	PRO194
D	MET195
D	EDO303
D	HOH440
D	HOH451
D	HOH459
D	HOH460
D	HOH487
D	HOH509
D	HOH605

site_id	AD3
Number of Residues	3
Details	binding site for residue EDO D 303

Chain	Residue
D	TYR158
D	NAD302
D	HOH446

site_id	AD4
Number of Residues	5
Details	binding site for residue EDO D 304

Chain	Residue
D	MET210
D	ARG248
D	MET249
D	GLN250
D	HOH551

site_id	AD5
Number of Residues	31
Details	binding site for residue NAD E 300

Chain	Residue
E	GLY12
E	SER15
E	GLY16
E	LEU17
E	ASP36
E	LEU37
E	CYS56
E	ASP57
E	VAL58
E	CYS83
E	ALA84
E	GLY85
E	THR143
E	ALA144
E	TYR158
E	LYS162
E	PRO188
E	GLY189
E	ILE190
E	PHE191
E	THR193
E	PRO194
E	MET195
E	EDO301
E	HOH441
E	HOH444
E	HOH460
E	HOH467
E	HOH468
E	HOH469
E	HOH610

site_id	AD6
Number of Residues	3
Details	binding site for residue EDO E 301

Chain	Residue
E	TYR158
E	NAD300
E	HOH602

site_id	AD7
Number of Residues	5
Details	binding site for residue EDO E 302

Chain	Residue
E	MET210
E	ARG248
E	MET249
E	GLN250
E	HOH609

site_id	AD8
Number of Residues	32
Details	binding site for residue NAD F 300

Chain	Residue
F	GLY12
F	SER15
F	GLY16
F	LEU17
F	ASP36
F	LEU37
F	CYS56
F	ASP57
F	VAL58
F	CYS83
F	ALA84
F	GLY85
F	VAL110
F	THR143
F	ALA144
F	TYR158
F	LYS162
F	PRO188
F	GLY189
F	ILE190
F	PHE191
F	THR193
F	PRO194
F	MET195
F	EDO301
F	HOH443
F	HOH444
F	HOH461
F	HOH473
F	HOH476
F	HOH481
F	HOH496

site_id	AD9
Number of Residues	4
Details	binding site for residue EDO F 301

Chain	Residue
F	TYR158
F	NAD300
F	HOH477
F	HOH601

site_id	AE1
Number of Residues	4
Details	binding site for residue EDO F 302

Chain	Residue
F	MET210
F	ARG248
F	MET249
F	GLN250

site_id	AE2
Number of Residues	6
Details	binding site for residue GOL G 301

Chain	Residue
F	GLU239
F	VAL240
G	GLU239
G	VAL240
G	HOH429
G	HOH456

site_id	AE3
Number of Residues	32
Details	binding site for residue NAD G 302

Chain	Residue
G	GLY12
G	SER15
G	GLY16
G	LEU17
G	ASP36
G	LEU37
G	CYS56
G	ASP57
G	VAL58
G	CYS83
G	ALA84
G	GLY85
G	VAL110
G	THR143
G	ALA144
G	TYR158
G	LYS162
G	PRO188
G	GLY189
G	ILE190
G	PHE191
G	THR193
G	PRO194
G	MET195
G	EDO303
G	HOH439
G	HOH455
G	HOH467
G	HOH483
G	HOH510
G	HOH511
G	HOH578

site_id	AE4
Number of Residues	3
Details	binding site for residue EDO G 303

Chain	Residue
G	TYR158
G	NAD302
G	HOH457

site_id	AE5
Number of Residues	5
Details	binding site for residue EDO G 304

Chain	Residue
G	MET210
G	ILE247
G	ARG248
G	MET249
G	GLN250

site_id	AE6
Number of Residues	7
Details	binding site for residue GOL H 301

Chain	Residue
E	GLU239
E	VAL240
H	GLU239
H	VAL240
H	HOH461
H	HOH475
H	HOH608

site_id	AE7
Number of Residues	31
Details	binding site for residue NAD H 302

Chain	Residue
H	GLY12
H	SER15
H	GLY16
H	LEU17
H	ASP36
H	LEU37
H	CYS56
H	ASP57
H	VAL58
H	CYS83
H	ALA84
H	VAL110
H	THR143
H	ALA144
H	TYR158
H	LYS162
H	PRO188
H	GLY189
H	ILE190
H	PHE191
H	THR193
H	PRO194
H	MET195
H	EDO303
H	HOH449
H	HOH464
H	HOH479
H	HOH483
H	HOH540
H	HOH548
H	HOH605

site_id	AE8
Number of Residues	4
Details	binding site for residue EDO H 303

Chain	Residue
H	TYR158
H	NAD302
H	HOH465
H	HOH588

site_id	AE9
Number of Residues	4
Details	binding site for residue EDO H 304

Chain	Residue
H	ARG248
H	MET249
H	GLN250
H	HOH568

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	SER145-ALA173

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