1HDA

A NOVEL ALLOSTERIC MECHANISM IN HAEMOGLOBIN. STRUCTURE OF BOVINE DEOXYHAEMOGLOBIN, ABSENCE OF SPECIFIC CHLORIDE-BINDING SITES AND ORIGIN OF THE CHLORIDE-LINKED BOHR EFFECT IN BOVINE AND HUMAN HAEMOGLOBIN

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	0005515	molecular_function	protein 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	0098869	biological_process	cellular oxidant detoxification
B	0004601	molecular_function	peroxidase activity
B	0005344	molecular_function	oxygen carrier activity
B	0005833	cellular_component	hemoglobin complex
B	0015671	biological_process	oxygen transport
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0031720	molecular_function	haptoglobin binding
B	0031721	molecular_function	hemoglobin alpha binding
B	0031838	cellular_component	haptoglobin-hemoglobin complex
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0043177	molecular_function	organic acid binding
B	0046872	molecular_function	metal ion binding
B	0098869	biological_process	cellular oxidant detoxification
C	0004601	molecular_function	peroxidase activity
C	0005344	molecular_function	oxygen carrier activity
C	0005506	molecular_function	iron ion binding
C	0005515	molecular_function	protein 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	0098869	biological_process	cellular oxidant detoxification
D	0004601	molecular_function	peroxidase activity
D	0005344	molecular_function	oxygen carrier activity
D	0005833	cellular_component	hemoglobin complex
D	0015671	biological_process	oxygen transport
D	0019825	molecular_function	oxygen binding
D	0020037	molecular_function	heme binding
D	0031720	molecular_function	haptoglobin binding
D	0031721	molecular_function	hemoglobin alpha binding
D	0031838	cellular_component	haptoglobin-hemoglobin complex
D	0042744	biological_process	hydrogen peroxide catabolic process
D	0043177	molecular_function	organic acid binding
D	0046872	molecular_function	metal ion binding
D	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	A1
Number of Residues	1
Details

Chain	Residue
A	HIS87

---

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM A 143

Chain	Residue
A	HIS87
A	LEU91
A	VAL93
A	ASN97
A	PHE98
A	LEU101
A	LEU136
A	HOH762
A	HOH765
C	LYS61
A	TYR42
A	PHE43
A	HIS58
A	LYS61
A	LEU86

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM B 148

Chain	Residue
A	HIS72
A	ASP75
A	HOH772
B	PHE42
B	HIS63
B	LYS66
B	VAL67
B	SER70
B	HIS92
B	LEU96
B	ASN102
B	PHE103
B	LEU106
B	LEU141

---

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM C 143

Chain	Residue
A	HIS45
C	TYR42
C	PHE43
C	HIS45
C	HIS58
C	LYS61
C	LEU83
C	HIS87
C	LEU91
C	VAL93
C	ASN97
C	PHE98
C	LEU101
C	LEU136
C	HOH761
C	HOH774

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE HEM D 148

Chain	Residue
B	LYS8
D	PHE42
D	HIS63
D	VAL67
D	SER70
D	HIS92
D	LEU96
D	ASN102
D	PHE103
D	LEU141

---

site_id	B1
Number of Residues	1
Details

Chain	Residue
B	HIS92

---

site_id	C1
Number of Residues	1
Details

Chain	Residue
C	HIS87

---

site_id	D1
Number of Residues	1
Details

Chain	Residue
D	HIS92

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: distal binding residue

Chain	Residue	Details
B	HIS63
D	HIS63

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: proximal binding residue

Chain	Residue	Details
B	HIS92
D	HIS92

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P68871

Chain	Residue	Details
B	THR12
D	THR12
A	HIS50
C	ALA4
C	PHE36
C	HIS50

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P68871

Chain	Residue	Details
B	SER44
D	SER44
A	THR41
C	GLY8
C	ALA12
C	THR41

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871

Chain	Residue	Details
B	LYS59
B	LYS82
D	LYS59
D	LYS82

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871

Chain	Residue	Details
B	CYS93
D	CYS93

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P01942

Chain	Residue	Details
A	HIS103
A	LEU125
A	LYS139
C	HIS103
C	LEU125
C	LYS139

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P01942

Chain	Residue	Details
A	LEU109
A	VAL135
A	SER138
C	LEU109
C	VAL135
C	SER138

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