2Q2N

Crystal structure of Bacillus subtilis ferrochelatase in complex with deuteroporphyrin IX 2,4-disulfonic acid dihydrochloride

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 1000

Chain	Residue
A	HOH9002
A	HOH9003
A	HOH9004
A	HOH9005
A	HOH9006
A	HOH9007

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 2000

Chain	Residue
A	HOH9011
A	HOH9012
A	HOH9013
A	HOH9008
A	HOH9009
A	HOH9010

---

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE H01 A 9001

Chain	Residue
A	TYR13
A	ILE29
A	ARG30
A	ARG31
A	ARG33
A	MET39
A	PHE120
A	HIS183
A	SER184
A	LEU185
A	PRO195
A	GLN199
A	GLY224
A	ASN225
A	THR226
A	PRO227
A	TRP230
A	HOH9032
A	HOH9068
A	HOH9093
A	HOH9127
A	HOH9181

---

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

---

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

---

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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