3QVZ

Crystal structure of the Zn-RIDC1 complex stabilized by BMOE crosslinks cocrystallized in the presence of Cu(II)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0009055	molecular_function	electron transfer activity
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0042597	cellular_component	periplasmic space
B	0005506	molecular_function	iron ion binding
B	0009055	molecular_function	electron transfer activity
B	0020037	molecular_function	heme binding
B	0022900	biological_process	electron transport chain
B	0042597	cellular_component	periplasmic space
C	0005506	molecular_function	iron ion binding
C	0009055	molecular_function	electron transfer activity
C	0020037	molecular_function	heme binding
C	0022900	biological_process	electron transport chain
C	0042597	cellular_component	periplasmic space
D	0005506	molecular_function	iron ion binding
D	0009055	molecular_function	electron transfer activity
D	0020037	molecular_function	heme binding
D	0022900	biological_process	electron transport chain
D	0042597	cellular_component	periplasmic space

Functional Information from PDB Data

site_id	AC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE HEM A 150

Chain	Residue
A	GLU4
A	MET7
A	PHE61
A	CYS98
A	CYS101
A	HIS102
A	ARG106
C	CU107
C	CU109

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ME7 A 501

Chain	Residue
A	ASN80
A	CYS82
C	CYS82

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 500

Chain	Residue
A	HIS73
A	HIS77
C	ASP74
D	HIS63

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU A 107

Chain	Residue
A	ALA1
A	ASP39
B	ASP2
B	ASP5

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU A 108

Chain	Residue
A	ASP2
A	ASP5
A	CU109
A	CU110
B	GLU4
B	HEM150

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU A 109

Chain	Residue
A	ASP5
A	CU108
A	CU110
B	HEM150
C	GLU4
C	HEM150

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU A 110

Chain	Residue
A	ASP2
A	ASP5
A	CU108
A	CU109
B	HEM150
C	GLU4

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 111

Chain	Residue
A	GLU8
A	ASP12
C	GLU8
C	ASP12

---

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM B 150

Chain	Residue
A	CU108
A	CU109
A	CU110
B	GLU4
B	MET7
B	PHE61
B	PHE65
B	LEU68
B	CYS98
B	CYS101
B	HIS102
C	HEM150

---

site_id	BC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ME7 B 501

Chain	Residue
B	ASP50
B	ASN80
B	GLU81
B	CYS82
D	ASP50
D	GLU81
D	CYS82

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 500

Chain	Residue
B	HIS73
B	HIS77
C	HIS63
D	ASP74

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 500

Chain	Residue
A	ASP74
B	HIS63
C	HIS73
C	HIS77

---

site_id	BC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE HEM C 150

Chain	Residue
A	CU109
B	HEM150
C	GLU4
C	MET7
C	PRO46
C	PHE61
C	CYS98
C	CYS101
C	HIS102
C	ARG106

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CU C 107

Chain	Residue
A	HEM150
C	ASP5
C	CU108
C	CU109
C	HOH112

---

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CU C 108

Chain	Residue
C	ASP5
C	CU107
C	CU109
C	HOH112
D	GLU4
D	HEM150

---

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CU C 109

Chain	Residue
A	HEM150
C	ASP2
C	ASP5
C	CU107
C	CU108
C	HOH113
D	HEM150

---

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CU C 110

Chain	Residue
D	ASP2
D	ASP5
C	ALA1
C	ASP39

---

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 500

Chain	Residue
A	HIS63
B	ASP74
D	HIS73
D	HIS77

---

site_id	CC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM D 150

Chain	Residue
C	ASP2
C	CU108
C	CU109
D	GLU4
D	MET7
D	ASN11
D	PRO46
D	PHE61
D	GLY64
D	CYS98
D	CYS101
D	HIS102

---