Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1U8V

Crystal Structure of 4-Hydroxybutyryl-CoA Dehydratase from Clostridium aminobutyricum: Radical catalysis involving a [4Fe-4S] cluster and flavin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0016491	molecular_function	oxidoreductase activity
A	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0043721	molecular_function	4-hydroxybutanoyl-CoA dehydratase activity
A	0046872	molecular_function	metal ion binding
A	0050393	molecular_function	vinylacetyl-CoA delta-isomerase activity
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0003824	molecular_function	catalytic activity
B	0016491	molecular_function	oxidoreductase activity
B	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0043721	molecular_function	4-hydroxybutanoyl-CoA dehydratase activity
B	0046872	molecular_function	metal ion binding
B	0050393	molecular_function	vinylacetyl-CoA delta-isomerase activity
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0003824	molecular_function	catalytic activity
C	0016491	molecular_function	oxidoreductase activity
C	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
C	0016829	molecular_function	lyase activity
C	0016853	molecular_function	isomerase activity
C	0043721	molecular_function	4-hydroxybutanoyl-CoA dehydratase activity
C	0046872	molecular_function	metal ion binding
C	0050393	molecular_function	vinylacetyl-CoA delta-isomerase activity
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0003824	molecular_function	catalytic activity
D	0016491	molecular_function	oxidoreductase activity
D	0016627	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors
D	0016829	molecular_function	lyase activity
D	0016853	molecular_function	isomerase activity
D	0043721	molecular_function	4-hydroxybutanoyl-CoA dehydratase activity
D	0046872	molecular_function	metal ion binding
D	0050393	molecular_function	vinylacetyl-CoA delta-isomerase activity
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE SF4 A 491

Chain	Residue
A	CYS99
A	PHE100
A	GLN101
A	CYS103
A	HIS292
A	SER295
A	CYS299

site_id	AC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD A 492

Chain	Residue
A	LYS153
A	ARG156
A	HIS188
A	GLN189
A	THR190
A	GLU455
A	HIS458
A	SER462
A	HOH6207
A	HOH6366
A	HOH6398
A	HOH6473
A	HOH6995
A	HOH8186
A	HOH8628
B	ALA323
B	HIS325
B	ASP386
B	ILE387
B	GLY389
B	GLY390
B	HOH6027
B	HOH6260
B	HOH6293
B	HOH6403
A	MET149
A	THR150

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 491

Chain	Residue
B	CYS99
B	PHE100
B	CYS103
B	HIS292
B	SER295
B	CYS299
B	GLU455
B	HOH8832

site_id	AC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD B 492

Chain	Residue
A	ALA323
A	HIS325
A	ASP386
A	ILE387
A	GLY389
A	GLY390
A	HOH6006
A	HOH6016
A	HOH6238
B	MET149
B	THR150
B	LYS153
B	ARG156
B	HIS188
B	GLN189
B	THR190
B	GLU455
B	HIS458
B	SER462
B	HOH6179
B	HOH6252
B	HOH6294
B	HOH6354
B	HOH6433
B	HOH6715
B	HOH6758
B	HOH6829
B	HOH7008
B	HOH7861
B	HOH8523

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 C 491

Chain	Residue
C	CYS99
C	PHE100
C	GLN101
C	CYS103
C	HIS292
C	SER295
C	CYS299
C	GLU455

site_id	AC6
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD C 492

Chain	Residue
C	HOH7559
C	HOH7597
D	ALA323
D	HIS325
D	ASP386
D	ILE387
D	GLY389
D	GLY390
D	HOH6132
D	HOH6159
D	HOH6175
C	MET149
C	THR150
C	LYS153
C	ARG156
C	HIS188
C	GLN189
C	THR190
C	GLU455
C	HIS458
C	SER462
C	HOH6046
C	HOH6093
C	HOH6168
C	HOH6242
C	HOH6421
C	HOH6773
C	HOH6944
C	HOH7193
C	HOH7264

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 D 491

Chain	Residue
D	CYS99
D	PHE100
D	GLN101
D	CYS103
D	HIS292
D	SER295
D	CYS299
D	GLU455

site_id	AC8
Number of Residues	27
Details	BINDING SITE FOR RESIDUE FAD D 492

Chain	Residue
C	ALA323
C	HIS325
C	ASP386
C	ILE387
C	GLY389
C	GLY390
C	HOH6037
C	HOH6170
C	HOH6176
D	MET149
D	THR150
D	LYS153
D	ARG156
D	HIS188
D	GLN189
D	THR190
D	GLU455
D	HIS458
D	HOH6169
D	HOH6171
D	HOH6314
D	HOH6361
D	HOH6381
D	HOH6508
D	HOH6641
D	HOH7196
D	HOH8235

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	72
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15496473","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 15496473

Chain	Residue	Details
A	HIS292

site_id	CSA2
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 15496473

Chain	Residue	Details
B	HIS292

site_id	CSA3
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 15496473

Chain	Residue	Details
C	HIS292

site_id	CSA4
Number of Residues	1
Details	a catalytic site defined by CSA, PubMed 15496473

Chain	Residue	Details
D	HIS292

site_id	MCSA1
Number of Residues	8
Details	M-CSA 750

Chain	Residue	Details
A	CYS99
A	CYS103
A	THR190	proton acceptor, proton donor, proton relay
A	GLU257	proton acceptor
A	HIS292	proton acceptor
A	TYR296	electrostatic stabiliser, radical stabiliser
A	CYS299
A	GLU455	proton donor

site_id	MCSA2
Number of Residues	8
Details	M-CSA 750

Chain	Residue	Details
B	CYS99
B	CYS103
B	THR190	proton acceptor, proton donor, proton relay
B	GLU257	proton acceptor
B	HIS292	proton acceptor
B	TYR296	electrostatic stabiliser, radical stabiliser
B	CYS299
B	GLU455	proton donor

site_id	MCSA3
Number of Residues	8
Details	M-CSA 750

Chain	Residue	Details
C	CYS99
C	CYS103
C	THR190	proton acceptor, proton donor, proton relay
C	GLU257	proton acceptor
C	HIS292	proton acceptor
C	TYR296	electrostatic stabiliser, radical stabiliser
C	CYS299
C	GLU455	proton donor

site_id	MCSA4
Number of Residues	8
Details	M-CSA 750

Chain	Residue	Details
D	CYS99
D	CYS103
D	THR190	proton acceptor, proton donor, proton relay
D	GLU257	proton acceptor
D	HIS292	proton acceptor
D	TYR296	electrostatic stabiliser, radical stabiliser
D	CYS299
D	GLU455	proton donor

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