1L8X

Crystal Structure of Ferrochelatase from the Yeast, Saccharomyces cerevisiae, with Cobalt(II) as the Substrate Ion

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004325	molecular_function	ferrochelatase activity
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005743	cellular_component	mitochondrial inner membrane
A	0006779	biological_process	porphyrin-containing compound biosynthetic process
A	0006783	biological_process	heme biosynthetic process
A	0016829	molecular_function	lyase activity
B	0004325	molecular_function	ferrochelatase activity
B	0005515	molecular_function	protein binding
B	0005739	cellular_component	mitochondrion
B	0005743	cellular_component	mitochondrial inner membrane
B	0006779	biological_process	porphyrin-containing compound biosynthetic process
B	0006783	biological_process	heme biosynthetic process
B	0016829	molecular_function	lyase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CO A 501

Chain	Residue
A	HIS235

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CO B 502

Chain	Residue
B	HIS235
B	GLU314

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Functional Information from PROSITE/UniProt

site_id	PS00534
Number of Residues	21
Details	FERROCHELATASE Ferrochelatase signature. LLfSaHSLPmdvv.NtGDayp.A

Chain	Residue	Details
A	LEU230-ALA250

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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Catalytic Information from CSA

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

Chain	Residue	Details
A	GLU314
A	HIS312
A	HIS235

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

Chain	Residue	Details
B	GLU314
B	HIS312
B	HIS235

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