3QQR

Crystal structure of Parasponia hemoglobin; Differential Heme Coordination is Linked to Quaternary Structure

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005344	molecular_function	oxygen carrier activity
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
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	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM A 163

Chain	Residue
A	LEU50
A	HIS105
A	VAL110
A	HIS114
A	PHE115
A	THR118
A	TYR146
A	LEU149
A	HOH178
A	HOH189
A	PHE51
A	TYR53
A	LYS66
A	HIS70
A	THR73
A	ARG100
A	ILE101
A	ILE104

---

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM B 163

Chain	Residue
B	LEU50
B	PHE51
B	SER52
B	HIS70
B	ARG100
B	ILE104
B	HIS105
B	THR108
B	VAL110
B	HIS114
B	PHE115
B	THR118
B	LEU149
B	ILE153
B	HOH221

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DIO A 164

Chain	Residue
A	LYS127
A	TRP134
A	LYS139
B	HOH188

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DIO A 165

Chain	Residue
A	ARG119
A	LYS139
A	ASN140
A	HOH194

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DIO B 164

Chain	Residue
B	LYS127
B	TRP134
B	LYS139

---

site_id	AC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DIO A 166

Chain	Residue
A	PHE115
A	GLU116
A	ARG119
A	TYR146
A	ASP147
A	VAL150
A	LYS154
A	HOH227

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DIO A 167

Chain	Residue
A	GLU12
A	GLU13
A	ARG86
A	HOH232
B	SER52
B	TYR53

---

Functional Information from PROSITE/UniProt

site_id	PS00208
Number of Residues	12
Details	PLANT_GLOBIN Plant hemoglobins signature. NPkLkpHAttvF

Chain	Residue	Details
A	ASN64-PHE75

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	Motif: {"description":"Homodimerization","evidences":[{"source":"PubMed","id":"21491905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QQR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21491905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QQR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"O04986","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"description":"distal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21491905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QQR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21491905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QQR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Site: {"description":"Homodimerization","evidences":[{"source":"PubMed","id":"21491905","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QQR","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---