2QMB

Structure determination of haemoglobin from Turkey(meleagris gallopavo) at 2.8 Angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0005344	molecular_function	oxygen carrier activity
A	0005506	molecular_function	iron ion binding
A	0005833	cellular_component	hemoglobin complex
A	0015671	biological_process	oxygen transport
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0031720	molecular_function	haptoglobin binding
A	0031838	cellular_component	haptoglobin-hemoglobin complex
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0043177	molecular_function	organic acid binding
A	0046872	molecular_function	metal ion binding
A	0072562	cellular_component	blood microparticle
A	0098869	biological_process	cellular oxidant detoxification
B	0005833	cellular_component	hemoglobin complex
B	0015671	biological_process	oxygen transport
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
C	0004601	molecular_function	peroxidase activity
C	0005344	molecular_function	oxygen carrier activity
C	0005506	molecular_function	iron ion binding
C	0005833	cellular_component	hemoglobin complex
C	0015671	biological_process	oxygen transport
C	0019825	molecular_function	oxygen binding
C	0020037	molecular_function	heme binding
C	0031720	molecular_function	haptoglobin binding
C	0031838	cellular_component	haptoglobin-hemoglobin complex
C	0042744	biological_process	hydrogen peroxide catabolic process
C	0043177	molecular_function	organic acid binding
C	0046872	molecular_function	metal ion binding
C	0072562	cellular_component	blood microparticle
C	0098869	biological_process	cellular oxidant detoxification
D	0005833	cellular_component	hemoglobin complex
D	0015671	biological_process	oxygen transport
D	0019825	molecular_function	oxygen binding
D	0020037	molecular_function	heme binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM A 150

Chain	Residue
A	TYR42
A	PHE98
A	LEU136
A	PHE43
A	HIS45
A	PHE46
A	HIS58
A	LYS61
A	LEU83
A	HIS87
A	ASN97

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM B 150

Chain	Residue
A	LYS16
B	PHE41
B	PHE42
B	PHE45
B	HIS63
B	LYS66
B	SER70
B	LEU88
B	HIS92
B	LEU96
B	LEU106

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE HEM C 150

Chain	Residue
C	TYR42
C	HIS45
C	HIS58
C	LYS61
C	LEU83
C	LEU86
C	HIS87
C	ASN97
C	PHE98
C	LEU101

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM D 150

Chain	Residue
D	THR38
D	PHE41
D	PHE42
D	PHE45
D	HIS63
D	LYS66
D	LEU88
D	HIS92
D	LEU96
D	ASN102
D	LEU106
D	LEU141

---

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE OXY A 151

Chain	Residue
A	HIS58

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OXY B 151

Chain	Residue
B	PHE42
B	HIS63

---

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OXY C 151

Chain	Residue
C	HIS58
C	HIS87

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE OXY D 151

Chain	Residue
D	HIS63
D	HIS92

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00238

Chain	Residue	Details
A	HIS58
C	HIS58

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: proximal binding residue => ECO:0000255|PROSITE-ProRule:PRU00238

Chain	Residue	Details
A	HIS87
C	HIS87

---