4F4D

F337R variant of human ferrochelatase

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 501

Chain	Residue
A	TYR123
A	SER130
A	ILE132
A	ILE342

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 502

Chain	Residue
A	HOH678
B	PRO277
B	GLN278
B	SER281
B	TRP301
A	PRO277
A	GLN278
A	SER281
A	TRP301
A	HOH604

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES A 503

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

---

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE CHD A 504

Chain	Residue
A	LEU89
A	LEU92
A	LEU98
A	ARG115
A	GLN122
A	HIS263
A	VAL305
A	HOH674
A	HOH691
A	HOH704
A	HOH735
A	HOH832
A	HOH844

---

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CHD A 505

Chain	Residue
A	MET99
A	ARG114
A	ARG115
A	VAL305
A	MET308
A	TRP310
A	CHD506
A	HOH705
A	HOH724
A	HOH771
A	HOH871

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CHD A 506

Chain	Residue
A	THR100
A	CHD505
A	HOH880
B	PHE110

---

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 501

Chain	Residue
B	TYR123
B	SER130
B	ILE132
B	ILE342

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FES B 502

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

---

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CHD B 503

Chain	Residue
B	MET99
B	ILE111
B	ARG114
B	ARG115
B	PRO266
B	MET308
B	CHD504
B	CHD505
B	HOH740
B	HOH855
B	HOH879

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CHD B 504

Chain	Residue
A	LYS106
A	PHE110
B	THR100
B	CHD503

---

site_id	BC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE CHD B 505

Chain	Residue
B	LEU98
B	ARG115
B	LYS118
B	ILE119
B	SER197
B	THR198
B	HIS263
B	VAL305
B	CHD503
B	HOH746
B	HOH795
B	HOH812
B	HOH837
B	HOH852
B	HOH859

---

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	4
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:11175906

Chain	Residue	Details
A	HIS230
A	ASP383
B	HIS230
B	ASP383

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:17261801, ECO:0007744|PDB:2HRE

Chain	Residue	Details
A	ARG115
A	TYR123
A	SER130
B	ARG115
B	TYR123
B	SER130

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:11175906, ECO:0000269|PubMed:17261801, ECO:0007744|PDB:1HRK, ECO:0007744|PDB:2HRC

Chain	Residue	Details
A	CYS196
B	CYS196

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:11175906, ECO:0007744|PDB:1HRK

Chain	Residue	Details
A	CYS403
A	CYS406
A	CYS411
B	CYS403
B	CYS406
B	CYS411

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P22315

Chain	Residue	Details
A	LYS138
B	LYS138

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P22315

Chain	Residue	Details
A	LYS415
B	LYS415

---

Catalytic Information from CSA

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	GLU343	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	GLU343	metal ligand, proton acceptor
B	GLU347

---