1F5O

2.9 ANGSTROM CRYSTAL STRUCTURE OF DEOXYGENATED LAMPREY HEMOGLOBIN V IN THE SPACE GROUP P2(1)2(1)2(1)

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	0016491	molecular_function	oxidoreductase activity
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
B	0005344	molecular_function	oxygen carrier activity
B	0005506	molecular_function	iron ion binding
B	0015671	biological_process	oxygen transport
B	0016491	molecular_function	oxidoreductase activity
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
C	0005344	molecular_function	oxygen carrier activity
C	0005506	molecular_function	iron ion binding
C	0015671	biological_process	oxygen transport
C	0016491	molecular_function	oxidoreductase activity
C	0019825	molecular_function	oxygen binding
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
D	0005344	molecular_function	oxygen carrier activity
D	0005506	molecular_function	iron ion binding
D	0015671	biological_process	oxygen transport
D	0016491	molecular_function	oxidoreductase activity
D	0019825	molecular_function	oxygen binding
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
E	0005344	molecular_function	oxygen carrier activity
E	0005506	molecular_function	iron ion binding
E	0015671	biological_process	oxygen transport
E	0016491	molecular_function	oxidoreductase activity
E	0019825	molecular_function	oxygen binding
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
F	0005344	molecular_function	oxygen carrier activity
F	0005506	molecular_function	iron ion binding
F	0015671	biological_process	oxygen transport
F	0016491	molecular_function	oxidoreductase activity
F	0019825	molecular_function	oxygen binding
F	0020037	molecular_function	heme binding
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM A 150

Chain	Residue
A	PHE51
A	PHE109
A	VAL111
A	TYR115
A	LEU119
A	PHE52
A	LYS54
A	HIS73
A	ARG76
A	ILE77
A	ALA80
A	LYS104
A	HIS105

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM B 150

Chain	Residue
B	PHE51
B	PHE52
B	LYS54
B	HIS73
B	ARG76
B	ALA80
B	LYS104
B	HIS105
B	PHE109
B	VAL111
B	TYR115
B	PHE116
B	LEU119

---

site_id	AC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM C 150

Chain	Residue
C	PHE51
C	PHE52
C	LYS54
C	HIS73
C	ARG76
C	ALA80
C	LYS104
C	HIS105
C	PHE109
C	VAL111
C	PHE116
C	LEU119

---

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM D 150

Chain	Residue
D	PHE51
D	PHE52
D	LYS54
D	HIS73
D	ARG76
D	ALA80
D	LYS104
D	HIS105
D	PHE109
D	VAL111
D	TYR115
D	PHE116
D	LEU119

---

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM E 150

Chain	Residue
E	PHE51
E	PHE52
E	LYS54
E	HIS73
E	ARG76
E	ALA80
E	LYS104
E	HIS105
E	PHE109
E	VAL111
E	LEU119
E	LEU145

---

site_id	AC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM F 150

Chain	Residue
F	PHE51
F	PHE52
F	LYS54
F	HIS73
F	ARG76
F	ALA80
F	LYS104
F	HIS105
F	PHE109
F	VAL111
F	TYR115
F	PHE116
F	LEU119
F	LEU145

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: distal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:4032476

Chain	Residue	Details
A	HIS73
B	HIS73
C	HIS73
D	HIS73
E	HIS73
F	HIS73

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238, ECO:0000269|PubMed:4032476

Chain	Residue	Details
A	HIS105
B	HIS105
C	HIS105
D	HIS105
E	HIS105
F	HIS105

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