Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FXQ

Structure of coproheme decarboxylase from Listeria monocytogenes during turnover

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0006783	biological_process	heme biosynthetic process
A	0006785	biological_process	heme B biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0016634	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
A	0098869	biological_process	cellular oxidant detoxification
B	0004601	molecular_function	peroxidase activity
B	0006783	biological_process	heme biosynthetic process
B	0006785	biological_process	heme B biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0016634	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
B	0098869	biological_process	cellular oxidant detoxification
C	0004601	molecular_function	peroxidase activity
C	0006783	biological_process	heme biosynthetic process
C	0006785	biological_process	heme B biosynthetic process
C	0016491	molecular_function	oxidoreductase activity
C	0016634	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
C	0098869	biological_process	cellular oxidant detoxification
D	0004601	molecular_function	peroxidase activity
D	0006783	biological_process	heme biosynthetic process
D	0006785	biological_process	heme B biosynthetic process
D	0016491	molecular_function	oxidoreductase activity
D	0016634	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
D	0098869	biological_process	cellular oxidant detoxification
E	0004601	molecular_function	peroxidase activity
E	0006783	biological_process	heme biosynthetic process
E	0006785	biological_process	heme B biosynthetic process
E	0016491	molecular_function	oxidoreductase activity
E	0016634	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
E	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue NA A 301

Chain	Residue
A	ILE63
A	LEU64
A	GLY65
A	ALA68
A	ASP69
A	HOH401
B	GLU86

site_id	AC2
Number of Residues	22
Details	binding site for residue FEC A 302

Chain	Residue
A	TYR147
A	MET149
A	LYS151
A	HIS174
A	GLY175
A	GLY178
A	ARG179
A	GLN187
A	TRP200
A	LEU204
A	ILE215
A	MET219
A	SER225
A	PHE231
A	VOV303
A	HOH405
A	HOH409
A	HOH420
A	HOH451
D	HIS42
A	SER111
A	TYR113

site_id	AC3
Number of Residues	23
Details	binding site for residue VOV A 303

Chain	Residue
A	LEU110
A	SER111
A	TYR113
A	ARG133
A	TYR147
A	MET149
A	LYS151
A	TRP159
A	HIS174
A	GLY178
A	ARG179
A	VAL185
A	GLN187
A	TRP200
A	LEU204
A	ILE215
A	MET219
A	SER225
A	PHE231
A	FEC302
A	HOH405
A	HOH409
A	HOH451

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

Chain	Residue
A	GLU80
A	ASN83
A	ASN87
C	SER62
C	GLN244
C	LYS247
C	LEU248

site_id	AC5
Number of Residues	6
Details	binding site for residue NA B 301

Chain	Residue
B	ILE63
B	LEU64
B	GLY65
B	ALA68
B	HOH410
E	GLU86

site_id	AC6
Number of Residues	12
Details	binding site for residue FEC B 302

Chain	Residue
B	TYR147
B	MET149
B	HIS174
B	GLY178
B	GLN187
B	TRP200
B	LEU204
B	MET219
B	SER225
B	PHE231
B	VOV303
B	HOH402

site_id	AC7
Number of Residues	17
Details	binding site for residue VOV B 303

Chain	Residue
B	LEU110
B	SER111
B	ARG133
B	TYR147
B	MET149
B	TRP159
B	HIS174
B	GLY178
B	GLN187
B	TRP200
B	VAL202
B	LEU204
B	MET219
B	SER225
B	PHE231
B	FEC302
B	HOH402

site_id	AC8
Number of Residues	5
Details	binding site for residue MPD B 304

Chain	Residue
A	LEU248
B	GLU80
B	ASN83
B	ASN87
B	HOH401

site_id	AC9
Number of Residues	6
Details	binding site for residue NA A 305

Chain	Residue
A	GLU86
C	ILE63
C	LEU64
C	GLY65
C	ALA68
C	HOH404

site_id	AD1
Number of Residues	19
Details	binding site for residue FEC C 301

Chain	Residue
C	SER111
C	TYR113
C	ARG133
C	TYR147
C	MET149
C	TRP159
C	HIS174
C	GLY178
C	ARG179
C	GLN187
C	TRP200
C	LEU204
C	MET219
C	SER225
C	PHE231
C	VOV302
C	HOH402
C	HOH408
C	HOH456

site_id	AD2
Number of Residues	20
Details	binding site for residue VOV C 302

Chain	Residue
C	LEU110
C	SER111
C	TYR113
C	TYR147
C	MET149
C	TRP159
C	HIS174
C	GLY178
C	ARG179
C	VAL185
C	GLN187
C	TRP200
C	LEU204
C	ILE215
C	MET219
C	SER225
C	PHE231
C	FEC301
C	HOH402
C	HOH408

site_id	AD3
Number of Residues	6
Details	binding site for residue NA C 303

Chain	Residue
C	GLU86
D	ILE63
D	LEU64
D	GLY65
D	ALA68
D	HOH432

site_id	AD4
Number of Residues	25
Details	binding site for residue FEC D 301

Chain	Residue
D	LEU110
D	SER111
D	TYR113
D	ARG133
D	TYR147
D	MET149
D	LYS151
D	TRP159
D	ILE171
D	HIS174
D	GLY178
D	ARG179
D	GLN187
D	TRP200
D	LEU204
D	ILE215
D	MET219
D	SER225
D	PHE231
D	VOV302
D	HOH402
D	HOH412
D	HOH465
D	HOH474
D	HOH481

site_id	AD5
Number of Residues	23
Details	binding site for residue VOV D 302

Chain	Residue
D	GLU109
D	SER111
D	TYR113
D	TYR147
D	MET149
D	LYS151
D	TRP159
D	HIS174
D	GLY178
D	ARG179
D	VAL185
D	GLN187
D	TRP200
D	LEU204
D	ILE215
D	MET219
D	SER225
D	PHE231
D	FEC301
D	HOH402
D	HOH412
D	HOH465
D	HOH481

site_id	AD6
Number of Residues	3
Details	binding site for residue MPD D 303

Chain	Residue
C	ASN87
D	GLN244
D	LYS247

site_id	AD7
Number of Residues	6
Details	binding site for residue NA D 304

Chain	Residue
D	GLU86
E	ILE63
E	LEU64
E	GLY65
E	ALA68
E	HOH412

site_id	AD8
Number of Residues	16
Details	binding site for residue FEC E 301

Chain	Residue
E	SER111
E	TYR113
E	TYR147
E	MET149
E	TRP159
E	HIS174
E	GLY178
E	ARG179
E	GLN187
E	TRP200
E	LEU204
E	MET219
E	SER225
E	VOV302
E	HOH401
E	HOH428

site_id	AD9
Number of Residues	22
Details	binding site for residue VOV E 302

Chain	Residue
E	LEU110
E	SER111
E	TYR113
E	ARG133
E	TYR147
E	MET149
E	TRP159
E	HIS174
E	GLY178
E	ARG179
E	VAL185
E	GLN187
E	TRP200
E	LEU204
E	ILE215
E	MET219
E	SER225
E	PHE231
E	FEC301
E	HOH401
E	HOH428
E	HOH464

site_id	AE1
Number of Residues	5
Details	binding site for residue MPD E 303

Chain	Residue
B	GLN244
E	GLU84
E	ASN87
E	HOH442
E	HOH452

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01442","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31423350","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	35
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01442","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27758026","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LOQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	5
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01442","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27758026","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LOQ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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