1JWN

Crystal Structure of Scapharca inaequivalvis HbI, I114F Mutant Ligated to Carbon Monoxide.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005344	molecular_function	oxygen carrier activity
A	0005737	cellular_component	cytoplasm
A	0015671	biological_process	oxygen transport
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0042802	molecular_function	identical protein binding
A	0046872	molecular_function	metal ion binding
B	0005344	molecular_function	oxygen carrier activity
B	0005737	cellular_component	cytoplasm
B	0015671	biological_process	oxygen transport
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0042802	molecular_function	identical protein binding
B	0046872	molecular_function	metal ion binding
C	0005344	molecular_function	oxygen carrier activity
C	0005737	cellular_component	cytoplasm
C	0015671	biological_process	oxygen transport
C	0019825	molecular_function	oxygen binding
C	0020037	molecular_function	heme binding
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
D	0005344	molecular_function	oxygen carrier activity
D	0005737	cellular_component	cytoplasm
D	0015671	biological_process	oxygen transport
D	0019825	molecular_function	oxygen binding
D	0020037	molecular_function	heme binding
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM A 147

Chain	Residue
A	TYR50
A	ILE106
A	GLU110
A	PHE111
A	CMO148
A	HOH163
A	HOH188
B	LYS96
B	ASN100
B	HEM147
A	PHE51
A	ARG53
A	LEU54
A	LEU73
A	PHE97
A	ASN100
A	HIS101
A	ARG104

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO A 148

Chain	Residue
A	MET37
A	PHE51
A	HIS69
A	LEU73
A	HEM147

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM B 147

Chain	Residue
A	LYS96
A	ASN100
A	HEM147
B	TYR50
B	PHE51
B	ARG53
B	HIS69
B	PHE97
B	ASN100
B	HIS101
B	ARG104
B	ILE106
B	GLU110
B	PHE111
B	PHE114
B	CMO148
B	HOH183

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO B 148

Chain	Residue
B	MET37
B	PHE51
B	HIS69
B	LEU73
B	HEM147

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM C 147

Chain	Residue
C	TYR50
C	PHE51
C	ARG53
C	HIS69
C	LEU77
C	PHE97
C	ASN100
C	HIS101
C	ARG104
C	ILE106
C	PHE111
C	PHE114
C	CMO148
C	HOH177
D	LYS96
D	ASN100
D	HEM147

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO C 148

Chain	Residue
C	MET37
C	PHE51
C	HIS69
C	LEU73
C	HEM147

---

site_id	AC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM D 147

Chain	Residue
C	LYS96
C	ASN100
C	HEM147
D	TYR50
D	PHE51
D	ARG53
D	LEU54
D	HIS69
D	ALA76
D	PHE97
D	HIS101
D	ARG104
D	ILE106
D	GLU110
D	PHE111
D	PHE114
D	CMO148
D	HOH176
D	HOH183

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO D 148

Chain	Residue
D	MET37
D	PHE51
D	HIS69
D	LEU73
D	HEM147

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	548
Details	Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"description":"proximal binding residue"}

Chain

Residue

Details

---