1I4Y

THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII WILD TYPE METHEMERYTHRIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005344	molecular_function	oxygen carrier activity
A	0005506	molecular_function	iron ion binding
A	0015671	biological_process	oxygen transport
A	0046872	molecular_function	metal ion binding
A	0098771	biological_process	inorganic ion homeostasis
B	0005344	molecular_function	oxygen carrier activity
B	0005506	molecular_function	iron ion binding
B	0015671	biological_process	oxygen transport
B	0046872	molecular_function	metal ion binding
B	0098771	biological_process	inorganic ion homeostasis
C	0005344	molecular_function	oxygen carrier activity
C	0005506	molecular_function	iron ion binding
C	0015671	biological_process	oxygen transport
C	0046872	molecular_function	metal ion binding
C	0098771	biological_process	inorganic ion homeostasis
D	0005344	molecular_function	oxygen carrier activity
D	0005506	molecular_function	iron ion binding
D	0015671	biological_process	oxygen transport
D	0046872	molecular_function	metal ion binding
D	0098771	biological_process	inorganic ion homeostasis
E	0005344	molecular_function	oxygen carrier activity
E	0005506	molecular_function	iron ion binding
E	0015671	biological_process	oxygen transport
E	0046872	molecular_function	metal ion binding
E	0098771	biological_process	inorganic ion homeostasis
F	0005344	molecular_function	oxygen carrier activity
F	0005506	molecular_function	iron ion binding
F	0015671	biological_process	oxygen transport
F	0046872	molecular_function	metal ion binding
F	0098771	biological_process	inorganic ion homeostasis
G	0005344	molecular_function	oxygen carrier activity
G	0005506	molecular_function	iron ion binding
G	0015671	biological_process	oxygen transport
G	0046872	molecular_function	metal ion binding
G	0098771	biological_process	inorganic ion homeostasis
H	0005344	molecular_function	oxygen carrier activity
H	0005506	molecular_function	iron ion binding
H	0015671	biological_process	oxygen transport
H	0046872	molecular_function	metal ion binding
H	0098771	biological_process	inorganic ion homeostasis

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL D 114

Chain	Residue
D	HIS25
D	HIS54
D	LEU98
D	ILE102
D	ASP106
D	FEO604

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL E 114

Chain	Residue
E	LEU98
E	ASP106
E	FEO605
E	HIS25
E	LEU28
E	HIS54

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL B 114

Chain	Residue
B	HIS25
B	LEU28
B	HIS54
B	LEU98
B	ILE102
B	ASP106
B	FEO602

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL C 114

Chain	Residue
C	HIS25
C	HIS54
C	LEU98
C	ILE102
C	ASP106
C	FEO603

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL H 114

Chain	Residue
H	HIS25
H	LEU28
H	HIS54
H	LEU98
H	ILE102
H	ASP106
H	FEO608

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL G 114

Chain	Residue
G	HIS25
G	LEU28
G	HIS54
G	LEU98
G	ILE102
G	ASP106
G	FEO607

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL F 114

Chain	Residue
F	HIS25
F	LEU28
F	HIS54
F	LEU98
F	ASP106
F	FEO606

---

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL A 114

Chain	Residue
A	HIS25
A	LEU28
A	HIS54
A	LEU98
A	ASP106
A	FEO601

---

site_id	AC9
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FEO A 601

Chain	Residue
A	HIS25
A	HIS54
A	PHE55
A	GLU58
A	HIS73
A	HIS77
A	HIS101
A	ASP106
A	CL114

---

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FEO B 602

Chain	Residue
B	HIS25
B	HIS54
B	PHE55
B	GLU58
B	HIS73
B	HIS77
B	HIS101
B	ASP106
B	CL114

---

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FEO C 603

Chain	Residue
C	HIS25
C	HIS54
C	PHE55
C	GLU58
C	HIS73
C	HIS77
C	HIS101
C	ASP106
C	CL114

---

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FEO D 604

Chain	Residue
D	HIS25
D	HIS54
D	PHE55
D	GLU58
D	HIS73
D	HIS77
D	HIS101
D	ASP106
D	CL114

---

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FEO E 605

Chain	Residue
E	HIS25
E	HIS54
E	PHE55
E	GLU58
E	HIS73
E	HIS77
E	HIS101
E	ASP106
E	CL114

---

site_id	BC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FEO F 606

Chain	Residue
F	HIS73
F	HIS77
F	HIS101
F	ASP106
F	CL114
F	HIS25
F	HIS54
F	GLU58

---

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FEO G 607

Chain	Residue
G	HIS25
G	HIS54
G	GLU58
G	HIS73
G	HIS77
G	HIS101
G	ASP106
G	CL114

---

site_id	BC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FEO H 608

Chain	Residue
H	HIS25
H	HIS54
H	PHE55
H	GLU58
H	HIS73
H	HIS77
H	HIS101
H	ASP106
H	CL114

---

Functional Information from PROSITE/UniProt

site_id	PS00550
Number of Residues	24
Details	HEMERYTHRINS Hemerythrin family signature. HFlnEQvlMqasq...Yqfyde.HkkeH

Chain	Residue	Details
A	HIS54-HIS77

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	56
Details	BINDING: BINDING => ECO:0000269|PubMed:11372200, ECO:0007744|PDB:1I4Y, ECO:0007744|PDB:1I4Z

Chain	Residue	Details
A	HIS25
B	GLU58
B	HIS73
B	HIS77
B	HIS101
B	ASP106
C	HIS25
C	HIS54
C	GLU58
C	HIS73
C	HIS77
A	HIS54
C	HIS101
C	ASP106
D	HIS25
D	HIS54
D	GLU58
D	HIS73
D	HIS77
D	HIS101
D	ASP106
E	HIS25
A	GLU58
E	HIS54
E	GLU58
E	HIS73
E	HIS77
E	HIS101
E	ASP106
F	HIS25
F	HIS54
F	GLU58
F	HIS73
A	HIS73
F	HIS77
F	HIS101
F	ASP106
G	HIS25
G	HIS54
G	GLU58
G	HIS73
G	HIS77
G	HIS101
G	ASP106
A	HIS77
H	HIS25
H	HIS54
H	GLU58
H	HIS73
H	HIS77
H	HIS101
H	ASP106
A	HIS101
A	ASP106
B	HIS25
B	HIS54

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