Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2QD1

2.2 Angstrom Structure of the human ferrochelatase variant E343K with substrate bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004325	molecular_function	ferrochelatase activity
A	0006783	biological_process	heme biosynthetic process
B	0004325	molecular_function	ferrochelatase activity
B	0006783	biological_process	heme biosynthetic process
C	0004325	molecular_function	ferrochelatase activity
C	0006783	biological_process	heme biosynthetic process
D	0004325	molecular_function	ferrochelatase activity
D	0006783	biological_process	heme biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES A 1001

Chain	Residue
A	CYS196
A	SER402
A	CYS403
A	CYS406
A	CYS411
A	HOH1043

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FES B 1002

Chain	Residue
B	CYS406
B	CYS411
B	CYS196
B	SER402
B	CYS403

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES C 1003

Chain	Residue
C	CYS196
C	ARG272
C	SER402
C	CYS403
C	CYS406
C	CYS411

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES D 1004

Chain	Residue
D	CYS196
D	ARG272
D	SER402
D	CYS403
D	CYS406
D	CYS411

site_id	AC5
Number of Residues	23
Details	BINDING SITE FOR RESIDUE PP9 A 701

Chain	Residue
A	MET76
A	GLY77
A	GLY78
A	PHE88
A	LEU92
A	LEU98
A	ARG115
A	ILE119
A	TYR123
A	SER130
A	TYR191
A	SER197
A	THR198
A	HIS263
A	LEU265
A	TYR276
A	VAL305
A	TRP310
A	HIS341
A	ILE342
A	LYS343
A	HOH1097
A	HOH1115

site_id	AC6
Number of Residues	21
Details	BINDING SITE FOR RESIDUE PP9 B 702

Chain	Residue
B	MET76
B	GLY78
B	PHE88
B	LEU89
B	LEU92
B	LEU98
B	MET99
B	ARG115
B	ILE119
B	TYR123
B	SER130
B	THR198
B	HIS263
B	TYR276
B	VAL305
B	ALA336
B	HIS341
B	ILE342
B	LYS343
B	HOH1135
B	HOH1153

site_id	AC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PP9 D 703

Chain	Residue
C	ILE111
C	ARG114
C	PRO307
C	MET308
C	HOH1084
D	PRO102
D	PHE110
D	ARG114
D	PP9704
D	CHD801
D	HOH1136

site_id	AC8
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PP9 D 704

Chain	Residue
C	PRO102
C	LEU107
C	PHE110
D	ILE111
D	ARG114
D	PRO307
D	MET308
D	PP9703
D	CHD802
D	HOH1110

site_id	AC9
Number of Residues	22
Details	BINDING SITE FOR RESIDUE PP9 C 705

Chain	Residue
C	TYR191
C	SER197
C	THR198
C	HIS263
C	ALA336
C	PHE337
C	HIS341
C	ILE342
C	LYS343
C	HOH1042
C	HOH1074
C	MET76
C	GLY77
C	GLY78
C	PHE88
C	PHE93
C	LEU98
C	MET99
C	ARG115
C	ILE119
C	TYR123
C	SER130

site_id	BC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE PP9 D 706

Chain	Residue
D	MET76
D	GLY77
D	GLY78
D	PHE88
D	LEU89
D	LEU92
D	PHE93
D	LEU98
D	ARG115
D	ILE119
D	TYR123
D	SER130
D	TYR191
D	THR198
D	HIS263
D	PRO266
D	VAL305
D	TRP310
D	ALA336
D	PHE337
D	HIS341
D	ILE342
D	LYS343
D	HOH1064
D	HOH1090

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CHD D 801

Chain	Residue
C	ARG115
C	PRO307
C	HOH1054
C	HOH1084
D	PP9703
D	HOH1136

site_id	BC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CHD D 802

Chain	Residue
C	HOH1106
D	ARG115
D	GLY306
D	PRO307
D	PP9704

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE IMD D 901

Chain	Residue
B	PRO277
D	PRO277
D	SER281
D	TRP301
D	HOH1160

Functional Information from PROSITE/UniProt

site_id	PS00534
Number of Residues	19
Details	FERROCHELATASE Ferrochelatase signature. ILfSaHSLPmsvv.NrGDp...Y

Chain	Residue	Details
A	ILE258-TYR276

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE:

Chain	Residue	Details
A	HIS230
A	ASP383
B	HIS230
B	ASP383
C	HIS230
C	ASP383
D	HIS230
D	ASP383

site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING:

Chain	Residue	Details
A	CYS196
C	CYS403
C	CYS406
C	CYS411
D	CYS196
D	CYS403
D	CYS406
D	CYS411
A	CYS403
A	CYS406
A	CYS411
B	CYS196
B	CYS403
B	CYS406
B	CYS411
C	CYS196

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P22315

Chain	Residue	Details
A	LYS138
B	LYS138
C	LYS138
D	LYS138

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P22315

Chain	Residue	Details
A	LYS415
B	LYS415
C	LYS415
D	LYS415

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1hrk

Chain	Residue	Details
A	LYS343
A	HIS263
A	HIS341

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1hrk

Chain	Residue	Details
B	LYS343
B	HIS263
B	HIS341

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1hrk

Chain	Residue	Details
C	LYS343
C	HIS263
C	HIS341

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1hrk

Chain	Residue	Details
D	LYS343
D	HIS263
D	HIS341

site_id	MCSA1
Number of Residues	9
Details	M-CSA 578

Chain	Residue	Details
A	MET76
A	LEU92
A	LEU98
A	ARG164
A	TYR165
A	HIS263	metal ligand, proton acceptor
A	ASP340
A	LYS343	metal ligand, proton acceptor
A	GLU347

site_id	MCSA2
Number of Residues	9
Details	M-CSA 578

Chain	Residue	Details
B	MET76
B	LEU92
B	LEU98
B	ARG164
B	TYR165
B	HIS263	metal ligand, proton acceptor
B	ASP340
B	LYS343	metal ligand, proton acceptor
B	GLU347

site_id	MCSA3
Number of Residues	9
Details	M-CSA 578

Chain	Residue	Details
C	MET76
C	LEU92
C	LEU98
C	ARG164
C	TYR165
C	HIS263	metal ligand, proton acceptor
C	ASP340
C	LYS343	metal ligand, proton acceptor
C	GLU347

site_id	MCSA4
Number of Residues	9
Details	M-CSA 578

Chain	Residue	Details
D	MET76
D	LEU92
D	LEU98
D	ARG164
D	TYR165
D	HIS263	metal ligand, proton acceptor
D	ASP340
D	LYS343	metal ligand, proton acceptor
D	GLU347

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