1C9E

STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004325	molecular_function	ferrochelatase activity
A	0005737	cellular_component	cytoplasm
A	0006783	biological_process	heme biosynthetic process
A	0016829	molecular_function	lyase activity
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 900

Chain	Residue
A	HOH652
A	HOH653
A	HOH654
A	HOH655
A	HOH656
A	HOH657

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site_id	AC2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MP1 A 800

Chain	Residue
A	ARG31
A	PHE120
A	SER121
A	HIS183
A	LEU185
A	PRO186
A	LYS188
A	SER222
A	THR226
A	GLU264
A	HOH434
A	HOH452
A	HOH521
A	TYR13
A	TYR25
A	ILE29

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Functional Information from PROSITE/UniProt

site_id	PS00534
Number of Residues	19
Details	FERROCHELATASE Ferrochelatase signature. LIvSaHSLPekik.EfGDp...Y

Chain	Residue	Details
A	LEU178-TYR196

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:10704318, ECO:0007744|PDB:1C1H

Chain	Residue	Details
A	TYR13
A	ARG31
A	HIS183
A	LYS188

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751

Chain	Residue	Details
A	GLU20

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00323

Chain	Residue	Details
A	ARG30
A	SER54
A	TYR125

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:12761666

Chain	Residue	Details
A	ARG46
A	ASP268
A	GLU272

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site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000305|PubMed:12761666, ECO:0000305|PubMed:16140324, ECO:0000305|PubMed:17198378, ECO:0000305|PubMed:21052751

Chain	Residue	Details
A	GLU264

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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	GLU264
A	HIS262
A	HIS183

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