Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6CIQ

Pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica with coenzyme A bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005506	molecular_function	iron ion binding
A	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
A	0006979	biological_process	response to oxidative stress
A	0016491	molecular_function	oxidoreductase activity
A	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
A	0019164	molecular_function	pyruvate synthase activity
A	0022900	biological_process	electron transport chain
A	0030976	molecular_function	thiamine pyrophosphate binding
A	0046872	molecular_function	metal ion binding
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	0005506	molecular_function	iron ion binding
B	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
B	0006979	biological_process	response to oxidative stress
B	0016491	molecular_function	oxidoreductase activity
B	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
B	0019164	molecular_function	pyruvate synthase activity
B	0022900	biological_process	electron transport chain
B	0030976	molecular_function	thiamine pyrophosphate binding
B	0046872	molecular_function	metal ion binding
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	0005506	molecular_function	iron ion binding
C	0006086	biological_process	acetyl-CoA biosynthetic process from pyruvate
C	0006979	biological_process	response to oxidative stress
C	0016491	molecular_function	oxidoreductase activity
C	0016903	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors
C	0019164	molecular_function	pyruvate synthase activity
C	0022900	biological_process	electron transport chain
C	0030976	molecular_function	thiamine pyrophosphate binding
C	0046872	molecular_function	metal ion binding
C	0051536	molecular_function	iron-sulfur cluster binding
C	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 1201

Chain	Residue
A	TRP681
A	CYS686
A	ILE687
A	CYS689
A	ASN690
A	CYS692
A	CYS752

site_id	AC2
Number of Residues	8
Details	binding site for residue SF4 A 1202

Chain	Residue
A	ILE701
A	CYS742
A	THR743
A	CYS745
A	GLY746
A	CYS748
A	PRO679
A	CYS696

site_id	AC3
Number of Residues	5
Details	binding site for residue SF4 A 1203

Chain	Residue
A	CYS809
A	CYS812
A	GLU814
A	CYS837
A	CYS1075

site_id	AC4
Number of Residues	21
Details	binding site for residue TPP A 1204

Chain	Residue
A	PRO27
A	ILE28
A	GLU62
A	GLU814
A	GLY836
A	CYS837
A	PHE866
A	GLU867
A	GLY966
A	ASP967
A	GLY968
A	TRP969
A	THR995
A	VAL997
A	TYR998
A	SER999
A	ASN1000
A	THR1001
A	MG1205
A	HOH1303
A	HOH1310

site_id	AC5
Number of Residues	5
Details	binding site for residue MG A 1205

Chain	Residue
A	ASP967
A	THR995
A	VAL997
A	TPP1204
A	HOH1303

site_id	AC6
Number of Residues	16
Details	binding site for residue COA A 1206

Chain	Residue
A	THR29
A	LEU422
A	GLY423
A	SER424
A	ASP425
A	GLY426
A	THR427
A	VAL428
A	GLY429
A	TYR452
A	THR461
A	ARG554
A	ASN556
A	TYR587
A	ASN598
A	ASN1000

site_id	AC7
Number of Residues	8
Details	binding site for residue SF4 B 1201

Chain	Residue
B	TRP681
B	CYS686
B	ILE687
B	CYS689
B	ASN690
B	CYS692
B	CYS752
B	LEU759

site_id	AC8
Number of Residues	7
Details	binding site for residue SF4 B 1202

Chain	Residue
B	CYS696
B	ILE701
B	CYS742
B	THR743
B	CYS745
B	GLY746
B	CYS748

site_id	AC9
Number of Residues	5
Details	binding site for residue SF4 B 1203

Chain	Residue
B	CYS809
B	CYS812
B	GLU814
B	CYS837
B	CYS1075

site_id	AD1
Number of Residues	24
Details	binding site for residue TPP B 1204

Chain	Residue
B	TYR998
B	SER999
B	ASN1000
B	THR1001
B	MG1205
B	HOH1301
B	HOH1308
B	PRO27
B	ILE28
B	GLU62
B	GLN86
B	GLU814
B	THR835
B	GLY836
B	CYS837
B	PHE866
B	GLU867
B	GLY966
B	ASP967
B	GLY968
B	TRP969
B	ILE973
B	THR995
B	VAL997

site_id	AD2
Number of Residues	5
Details	binding site for residue MG B 1205

Chain	Residue
B	ASP967
B	THR995
B	VAL997
B	TPP1204
B	HOH1301

site_id	AD3
Number of Residues	15
Details	binding site for residue COA B 1206

Chain	Residue
B	THR29
B	ILE121
B	SER424
B	ASP425
B	GLY426
B	THR427
B	VAL428
B	GLY429
B	LYS456
B	ARG554
B	ASN556
B	TYR587
B	ASN598
B	ASN1000
B	HOH1308

site_id	AD4
Number of Residues	8
Details	binding site for residue SF4 C 1201

Chain	Residue
C	TRP681
C	CYS686
C	ILE687
C	CYS689
C	ASN690
C	CYS692
C	CYS752
C	ALA758

site_id	AD5
Number of Residues	7
Details	binding site for residue SF4 C 1202

Chain	Residue
C	CYS696
C	ILE701
C	CYS742
C	THR743
C	CYS745
C	GLY746
C	CYS748

site_id	AD6
Number of Residues	6
Details	binding site for residue SF4 C 1203

Chain	Residue
C	LYS456
C	CYS809
C	CYS812
C	GLU814
C	CYS837
C	CYS1075

site_id	AD7
Number of Residues	23
Details	binding site for residue TPP C 1204

Chain	Residue
C	PRO27
C	ILE28
C	GLU62
C	GLN86
C	GLU814
C	GLY836
C	CYS837
C	PHE866
C	GLU867
C	GLY966
C	ASP967
C	GLY968
C	TRP969
C	THR995
C	VAL997
C	TYR998
C	SER999
C	ASN1000
C	THR1001
C	MG1205
C	COA1206
C	HOH1301
C	HOH1303

site_id	AD8
Number of Residues	5
Details	binding site for residue MG C 1205

Chain	Residue
C	ASP967
C	THR995
C	VAL997
C	TPP1204
C	HOH1301

site_id	AD9
Number of Residues	21
Details	binding site for residue COA C 1206

Chain	Residue
C	THR29
C	ARG112
C	ILE121
C	GLY423
C	SER424
C	ASP425
C	GLY426
C	THR427
C	VAL428
C	TYR452
C	ASP453
C	LYS455
C	LYS456
C	ARG554
C	ASN556
C	VAL557
C	TYR587
C	ASN598
C	ASN1000
C	THR1001
C	TPP1204

Functional Information from PROSITE/UniProt

site_id	PS00198
Number of Residues	12
Details	4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiQCNqCSlVCP

Chain	Residue	Details
A	CYS686-PRO697
A	CYS742-PRO753

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	BINDING: BINDING => ECO:0000305\|PubMed:29581263, ECO:0000312\|PDB:6CIO

Chain	Residue	Details
A	THR29
A	ARG112
A	ASN1000
B	THR29
B	ARG112
B	ASN1000
C	THR29
C	ARG112
C	ASN1000

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:29581263, ECO:0000312\|PDB:6CIQ

Chain	Residue	Details
A	SER424
C	LYS456
C	ASN556
C	ASN598
A	LYS456
A	ASN556
A	ASN598
B	SER424
B	LYS456
B	ASN556
B	ASN598
C	SER424

site_id	SWS_FT_FI3
Number of Residues	45
Details	BINDING: BINDING => ECO:0000269\|PubMed:29581263, ECO:0000312\|PDB:6CIN

Chain	Residue	Details
A	CYS686
A	CYS812
A	CYS837
A	ASP967
A	THR995
A	VAL997
A	CYS1075
B	CYS686
B	CYS689
B	CYS692
B	CYS696
A	CYS689
B	CYS742
B	CYS745
B	CYS748
B	CYS752
B	CYS809
B	CYS812
B	CYS837
B	ASP967
B	THR995
B	VAL997
A	CYS692
B	CYS1075
C	CYS686
C	CYS689
C	CYS692
C	CYS696
C	CYS742
C	CYS745
C	CYS748
C	CYS752
C	CYS809
A	CYS696
C	CYS812
C	CYS837
C	ASP967
C	THR995
C	VAL997
C	CYS1075
A	CYS742
A	CYS745
A	CYS748
A	CYS752
A	CYS809

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:29581263, ECO:0000312\|PDB:6CIO

Chain	Residue	Details
A	GLU814
B	GLU814
C	GLU814

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