Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1SB3

Structure of 4-hydroxybenzoyl-CoA reductase from Thauera aromatica

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0016491	molecular_function	oxidoreductase activity
A	0018525	molecular_function	4-hydroxybenzoyl-CoA reductase activity
B	0016491	molecular_function	oxidoreductase activity
B	0018525	molecular_function	4-hydroxybenzoyl-CoA reductase activity
B	0046872	molecular_function	metal ion binding
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0071949	molecular_function	FAD binding
C	0016491	molecular_function	oxidoreductase activity
C	0018525	molecular_function	4-hydroxybenzoyl-CoA reductase activity
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0005506	molecular_function	iron ion binding
D	0016491	molecular_function	oxidoreductase activity
D	0018525	molecular_function	4-hydroxybenzoyl-CoA reductase activity
E	0016491	molecular_function	oxidoreductase activity
E	0018525	molecular_function	4-hydroxybenzoyl-CoA reductase activity
E	0046872	molecular_function	metal ion binding
E	0050660	molecular_function	flavin adenine dinucleotide binding
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0071949	molecular_function	FAD binding
F	0016491	molecular_function	oxidoreductase activity
F	0018525	molecular_function	4-hydroxybenzoyl-CoA reductase activity
F	0046872	molecular_function	metal ion binding
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 D 1112

Chain	Residue
D	ILE705
D	GLU706
D	VAL707
D	HOH2172

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 1113

Chain	Residue
E	ALA26
E	LEU28
E	GLY45
E	HIS46
E	TYR141

site_id	AC3
Number of Residues	40
Details	BINDING SITE FOR RESIDUE PCD A 1920

Chain	Residue
A	GLN214
A	GLY243
A	GLY244
A	PHE245
A	GLY246
A	THR249
A	MET357
A	ARG358
A	ILE481
A	GLY482
A	GLN483
A	GLY484
A	SER485
A	SER520
A	TYR521
A	SER522
A	SER523
A	ARG524
A	VAL525
A	THR526
A	VAL650
A	LYS652
A	LEU654
A	ASN655
A	ALA658
A	VAL659
A	GLN662
A	ALA721
A	LYS722
A	GLU723
A	ALA724
A	SER725
A	GLU726
A	HOH1923
A	HOH1965
A	HOH2011
A	HOH2049
A	HOH2071
C	GLN99
C	CYS137

site_id	AC4
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD B 1900

Chain	Residue
B	PRO29
B	GLY31
B	ALA32
B	GLY33
B	THR34
B	ASP35
B	LEU36
B	LEU53
B	LEU78
B	VAL101
B	ALA102
B	ALA110
B	THR111
B	GLY114
B	ASN115
B	CYS117
B	GLN118
B	GLY161
B	ASP162
B	LEU201
B	LEU207
B	LYS224
B	VAL231
B	ASP232
B	PHE233
B	HOH1932
B	HOH1942
B	HOH1959
B	HOH1969
C	GLY44

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SF4 B 1910

Chain	Residue
B	CYS122
B	CYS138
B	LYS140
B	CYS146
B	HIS147
B	CYS155
B	TYR156
B	ALA157

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES C 1907

Chain	Residue
A	MET191
C	GLN99
C	CYS100
C	GLY101
C	CYS103
C	CYS135
C	ARG136
C	CYS137

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES C 1908

Chain	Residue
C	CYS46
C	GLY47
C	CYS49
C	CYS61
C	GLY40
C	CYS41
C	GLY44
C	GLU45

site_id	AC8
Number of Residues	39
Details	BINDING SITE FOR RESIDUE PCD D 1921

Chain	Residue
D	GLN214
D	GLY243
D	GLY244
D	PHE245
D	GLY246
D	THR249
D	MET357
D	ARG358
D	ILE481
D	GLY482
D	GLN483
D	GLY484
D	SER485
D	SER520
D	TYR521
D	SER522
D	SER523
D	ARG524
D	VAL525
D	THR526
D	VAL650
D	LYS652
D	LEU654
D	ASN655
D	ALA658
D	VAL659
D	GLN662
D	ALA721
D	LYS722
D	GLU723
D	ALA724
D	SER725
D	GLU726
D	HOH1937
D	HOH1962
D	HOH2014
D	HOH2045
F	GLN99
F	CYS137

site_id	AC9
Number of Residues	30
Details	BINDING SITE FOR RESIDUE FAD E 1901

Chain	Residue
E	PRO29
E	GLY31
E	ALA32
E	GLY33
E	THR34
E	ASP35
E	LEU36
E	LEU53
E	LEU78
E	VAL101
E	ALA102
E	THR111
E	GLY114
E	ASN115
E	CYS117
E	GLN118
E	GLY161
E	ASP162
E	LEU201
E	LEU206
E	LEU207
E	LYS224
E	VAL231
E	ASP232
E	PHE233
E	HOH1918
E	HOH1928
E	HOH1965
E	HOH2007
F	GLY44

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SF4 E 1911

Chain	Residue
E	CYS122
E	PHE124
E	CYS138
E	LYS140
E	CYS146
E	HIS147
E	CYS155
E	TYR156
E	ALA157

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES F 1917

Chain	Residue
D	MET191
F	GLN99
F	CYS100
F	GLY101
F	CYS103
F	CYS135
F	ARG136
F	CYS137

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES F 1918

Chain	Residue
F	GLN39
F	GLY40
F	CYS41
F	GLY44
F	GLU45
F	CYS46
F	GLY47
F	CYS49
F	CYS61

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EPE A 1111

Chain	Residue
A	HIS453
A	TRP454
A	THR455
A	GLY456
A	HIS459
A	GLN605

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGFGARTEaLhfeiiagl..........LARK

Chain	Residue	Details
A	LEU241-LYS264

site_id	PS00197
Number of Residues	9
Details	2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CDGGECGAC

Chain	Residue	Details
C	CYS41-CYS49

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15576037","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RM6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	430
Details	Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15576037","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	24
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	152
Details	Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
A	GLU723

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
D	GLU723

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
A	GLN214
A	ARG358

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
D	GLN214
D	ARG358

site_id	CSA5
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
A	GLU726

site_id	CSA6
Number of Residues	1
Details	Annotated By Reference To The Literature 1fiq

Chain	Residue	Details
D	GLU726

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