Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FXJ

Structure of coproheme decarboxylase from Listeria monocytogenes in complex with iron coproporphyrin III

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	6
Details	binding site for residue NA A 301

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

site_id	AC2
Number of Residues	25
Details	binding site for residue FEC A 302

Chain	Residue
A	TYR147
A	MET149
A	LYS151
A	TRP159
A	ILE171
A	HIS174
A	GLY178
A	ARG179
A	GLN187
A	TRP200
A	LEU204
A	ILE215
A	MET219
A	SER225
A	HOH402
A	HOH407
A	HOH432
A	HOH439
A	HOH451
A	HOH459
A	HOH466
D	HIS42
A	SER111
A	TYR113
A	LEU114

site_id	AC3
Number of Residues	6
Details	binding site for residue NA B 301

Chain	Residue
B	ILE63
B	LEU64
B	GLY65
B	ALA68
B	ASP69
E	GLU86

site_id	AC4
Number of Residues	19
Details	binding site for residue FEC B 302

Chain	Residue
B	LEU110
B	SER111
B	ARG133
B	TYR147
B	MET149
B	LYS151
B	TRP159
B	ILE171
B	HIS174
B	GLY178
B	ARG179
B	GLN187
B	TRP200
B	LEU204
B	MET219
B	SER225
B	HOH422
B	HOH499
B	HOH546

site_id	AC5
Number of Residues	1
Details	binding site for residue POL B 303

Chain	Residue
B	SER233

site_id	AC6
Number of Residues	1
Details	binding site for residue POL B 304

Chain	Residue
B	ASP197

site_id	AC7
Number of Residues	7
Details	binding site for residue NA C 301

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

site_id	AC8
Number of Residues	16
Details	binding site for residue FEC C 302

Chain	Residue
C	SER111
C	ARG133
C	TYR147
C	MET149
C	LYS151
C	TRP159
C	HIS174
C	GLY178
C	GLN187
C	ILE189
C	TRP200
C	VAL202
C	ILE215
C	MET219
C	HOH407
C	HOH490

site_id	AC9
Number of Residues	4
Details	binding site for residue POL C 303

Chain	Residue
C	TYR102
C	SER233
C	HOH501
C	HOH510

site_id	AD1
Number of Residues	3
Details	binding site for residue POL C 305

Chain	Residue
C	GLN126
C	ASN127
C	HOH543

site_id	AD2
Number of Residues	4
Details	binding site for residue NA C 306

Chain	Residue
C	THR50
C	ARG76
C	HOH507
C	HOH569

site_id	AD3
Number of Residues	6
Details	binding site for residue NA D 301

Chain	Residue
C	GLU86
D	ILE63
D	GLY65
D	ALA68
D	ASP69
D	HOH408

site_id	AD4
Number of Residues	2
Details	binding site for residue POL D 303

Chain	Residue
D	HOH525
D	THR101

site_id	AD5
Number of Residues	5
Details	binding site for residue POL D 305

Chain	Residue
D	LYS67
D	THR101
D	SER233
D	HOH588
D	HOH666

site_id	AD6
Number of Residues	1
Details	binding site for residue CL D 307

Chain	Residue
D	ARG179

site_id	AD7
Number of Residues	6
Details	binding site for residue NA E 301

Chain	Residue
E	ILE63
E	LEU64
E	GLY65
E	ALA68
E	ASP69
E	HOH408

site_id	AD8
Number of Residues	20
Details	binding site for residue FEC E 302

Chain	Residue
E	SER111
E	TYR113
E	ARG133
E	TYR147
E	MET149
E	LYS151
E	TRP159
E	ILE171
E	HIS174
E	GLY178
E	ARG179
E	GLN187
E	TRP200
E	LEU204
E	MET219
E	SER225
E	HOH406
E	HOH412
E	HOH453
E	HOH543

site_id	AD9
Number of Residues	3
Details	binding site for residue POL E 303

Chain	Residue
E	TYR102
E	SER233
E	HOH403

site_id	AE1
Number of Residues	1
Details	binding site for residue POL E 304

Chain	Residue
E	ASP197

site_id	AE2
Number of Residues	32
Details	binding site for Di-peptide FEC D 302 and GLN D 187

Chain	Residue
B	HIS42
D	SER111
D	TYR113
D	TYR147
D	MET149
D	LYS151
D	TRP159
D	ILE171
D	HIS174
D	GLY178
D	ARG179
D	VAL185
D	GLN186
D	ILE188
D	TRP200
D	THR203
D	LEU204
D	ILE215
D	MET219
D	SER225
D	PHE231
D	HOH414
D	HOH419
D	HOH420
D	HOH430
D	HOH433
D	HOH435
D	HOH438
D	HOH457
D	HOH481
D	HOH504
D	HOH607

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)