Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ZAI

Crystal structure of 3-Hydroxypropionyl-CoA dehydratase from Metallosphaera sedula

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004300	molecular_function	enoyl-CoA hydratase activity
A	0006631	biological_process	fatty acid metabolic process
A	0006635	biological_process	fatty acid beta-oxidation
A	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
B	0003824	molecular_function	catalytic activity
B	0004300	molecular_function	enoyl-CoA hydratase activity
B	0006631	biological_process	fatty acid metabolic process
B	0006635	biological_process	fatty acid beta-oxidation
B	0016829	molecular_function	lyase activity
B	0016836	molecular_function	hydro-lyase activity
B	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
C	0003824	molecular_function	catalytic activity
C	0004300	molecular_function	enoyl-CoA hydratase activity
C	0006631	biological_process	fatty acid metabolic process
C	0006635	biological_process	fatty acid beta-oxidation
C	0016829	molecular_function	lyase activity
C	0016836	molecular_function	hydro-lyase activity
C	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
D	0003824	molecular_function	catalytic activity
D	0004300	molecular_function	enoyl-CoA hydratase activity
D	0006631	biological_process	fatty acid metabolic process
D	0006635	biological_process	fatty acid beta-oxidation
D	0016829	molecular_function	lyase activity
D	0016836	molecular_function	hydro-lyase activity
D	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
E	0003824	molecular_function	catalytic activity
E	0004300	molecular_function	enoyl-CoA hydratase activity
E	0006631	biological_process	fatty acid metabolic process
E	0006635	biological_process	fatty acid beta-oxidation
E	0016829	molecular_function	lyase activity
E	0016836	molecular_function	hydro-lyase activity
E	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity
F	0003824	molecular_function	catalytic activity
F	0004300	molecular_function	enoyl-CoA hydratase activity
F	0006631	biological_process	fatty acid metabolic process
F	0006635	biological_process	fatty acid beta-oxidation
F	0016829	molecular_function	lyase activity
F	0016836	molecular_function	hydro-lyase activity
F	0043956	molecular_function	3-hydroxypropionyl-CoA dehydratase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	20
Details	binding site for residue COA A 301

Chain	Residue
A	ASP23
A	PRO132
A	LEU136
A	HOH403
A	HOH405
A	HOH411
A	HOH420
A	HOH459
A	HOH510
A	HOH535
C	PHE248
A	LYS24
C	LYS251
A	LEU25
A	ALA63
A	ALA65
A	ASP66
A	ILE67
A	PHE70
A	LEU108

site_id	AC2
Number of Residues	6
Details	binding site for residue EDO A 302

Chain	Residue
A	GLU93
A	ASN214
A	HOH463
A	HOH480
A	HOH557
B	LYS154

site_id	AC3
Number of Residues	2
Details	binding site for residue EDO A 303

Chain	Residue
A	ARG21
A	ASP23

site_id	AC4
Number of Residues	7
Details	binding site for residue EDO A 304

Chain	Residue
A	LYS59
A	GLY105
A	TYR106
A	GLU126
A	ALA127
A	GLN128
A	HOH479

site_id	AC5
Number of Residues	5
Details	binding site for residue EDO A 305

Chain	Residue
A	THR74
D	ILE204
D	THR238
D	GLU239
D	HOH474

site_id	AC6
Number of Residues	8
Details	binding site for residue GOL A 306

Chain	Residue
A	LYS9
A	GLU11
A	TRP16
A	THR18
A	THR55
A	GLU188
A	ARG192
A	HOH464

site_id	AC7
Number of Residues	5
Details	binding site for residue GOL A 307

Chain	Residue
A	GLU159
A	MET160
A	ILE167
A	TYR175
C	HOH425

site_id	AC8
Number of Residues	12
Details	binding site for residue COA B 301

Chain	Residue
B	ASP23
B	LYS24
B	LEU25
B	ALA63
B	ALA65
B	ASP66
B	ILE67
B	PHE70
B	TYR106
B	LEU108
B	PRO132
B	ARG166

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO B 302

Chain	Residue
B	GLY105
B	TYR106
B	GLU126
B	ALA127
B	GLN128

site_id	AD1
Number of Residues	4
Details	binding site for residue GOL B 303

Chain	Residue
B	ARG156
B	GLU159
B	ILE167
B	TYR175

site_id	AD2
Number of Residues	15
Details	binding site for residue COA C 301

Chain	Residue
B	PHE248
B	LYS251
C	ASP23
C	LYS24
C	LEU25
C	ALA63
C	GLY64
C	ALA65
C	ASP66
C	ILE67
C	LEU108
C	GLY110
C	PRO132
C	ARG166
C	HOH482

site_id	AD3
Number of Residues	4
Details	binding site for residue EDO C 302

Chain	Residue
C	ARG156
C	GLU159
C	MET160
C	HOH404

site_id	AD4
Number of Residues	7
Details	binding site for residue GOL C 303

Chain	Residue
C	HOH470
A	LYS154
A	HOH509
C	GLU93
C	ARG150
C	ASN214
C	LEU217

site_id	AD5
Number of Residues	6
Details	binding site for residue GOL C 304

Chain	Residue
C	SER237
C	THR238
C	GLU239
C	LYS241
C	LYS242
C	HOH444

site_id	AD6
Number of Residues	8
Details	binding site for residue EDO D 301

Chain	Residue
D	GLU113
D	GLU133
D	PRO140
D	GLY141
D	TYR142
D	HOH476
D	HOH504
F	TRP232

site_id	AD7
Number of Residues	6
Details	binding site for residue EDO D 302

Chain	Residue
D	ASN13
D	LEU14
D	GLU196
D	ALA199
D	LYS200
D	HOH519

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO D 303

Chain	Residue
D	ARG156
D	GLU159
D	TYR175

site_id	AD9
Number of Residues	7
Details	binding site for residue GOL D 304

Chain	Residue
B	LYS9
D	GLU11
D	TRP16
D	THR18
D	THR55
D	GLU188
D	HOH503

site_id	AE1
Number of Residues	6
Details	binding site for residue GOL D 305

Chain	Residue
D	GLU93
D	ARG147
D	LEU217
D	HOH475
D	HOH482
E	LYS154

site_id	AE2
Number of Residues	6
Details	binding site for residue GOL D 306

Chain	Residue
B	GLU11
B	THR18
B	GLU188
B	ARG192
D	LYS9
D	HOH510

site_id	AE3
Number of Residues	12
Details	binding site for residue COA E 301

Chain	Residue
D	PHE248
E	ASP23
E	LYS24
E	LEU25
E	ALA63
E	ALA65
E	ASP66
E	ILE67
E	TYR106
E	PRO132
E	ARG166
E	HOH508

site_id	AE4
Number of Residues	8
Details	binding site for residue GOL E 302

Chain	Residue
D	ASN179
E	ARG156
E	GLU159
E	MET160
E	ASP165
E	ILE167
E	TYR175
E	HOH438

site_id	AE5
Number of Residues	4
Details	binding site for residue EDO F 301

Chain	Residue
F	ARG156
F	GLU159
F	ILE167
F	TYR175

site_id	AE6
Number of Residues	4
Details	binding site for residue EDO F 302

Chain	Residue
F	LYS9
F	THR18
F	GLU188
F	HOH492

site_id	AE7
Number of Residues	7
Details	binding site for residue GOL F 303

Chain	Residue
E	GLU93
E	ARG147
E	ASN214
E	HOH418
E	HOH445
F	LYS154
F	HOH424

Functional Information from PROSITE/UniProt

site_id	PS00166
Number of Residues	21
Details	ENOYL_COA_HYDRATASE Enoyl-CoA hydratase/isomerase signature. IAmINGyalGGGlelaLaCDI

Chain	Residue	Details
A	ILE100-ILE120

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	ACT_SITE: Nucleophile => ECO:0000250\|UniProtKB:Q5LLW6

Chain	Residue	Details
A	GLU113
B	GLU113
C	GLU113
D	GLU113
E	GLU113
F	GLU113

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: Proton acceptor => ECO:0000250\|UniProtKB:Q5LLW6

Chain	Residue	Details
A	GLU133
B	GLU133
C	GLU133
D	GLU133
E	GLU133
F	GLU133

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