3D4X

Crystal structure determination of cat (Felis silvestris catus) hemoglobin at 2.2 angstrom resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0031838	cellular_component	haptoglobin-hemoglobin complex
A	0046872	molecular_function	metal ion binding
A	0048821	biological_process	erythrocyte development
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	0031721	molecular_function	hemoglobin alpha binding
B	0031838	cellular_component	haptoglobin-hemoglobin complex
B	0046872	molecular_function	metal ion binding
B	0048821	biological_process	erythrocyte development
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	0031838	cellular_component	haptoglobin-hemoglobin complex
C	0046872	molecular_function	metal ion binding
C	0048821	biological_process	erythrocyte development
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	0031721	molecular_function	hemoglobin alpha binding
D	0031838	cellular_component	haptoglobin-hemoglobin complex
D	0046872	molecular_function	metal ion binding
D	0048821	biological_process	erythrocyte development

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM A 143

Chain	Residue
A	TYR42
A	LEU91
A	VAL93
A	ASN97
A	PHE98
A	LEU101
A	LEU136
A	HOH142
A	HOH155
A	PHE43
A	HIS45
A	PHE46
A	HIS58
A	LYS61
A	LEU83
A	LEU86
A	HIS87

---

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM B 148

Chain	Residue
B	PHE41
B	PHE42
B	HIS63
B	SER70
B	HIS92
B	LEU96
B	VAL98
B	ASN102
B	LEU106
B	LEU141
B	HOH151
B	HOH171

---

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

Chain	Residue
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	HOH142
C	HOH156
C	HOH179

---

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM D 148

Chain	Residue
D	THR38
D	PHE41
D	PHE42
D	HIS63
D	LYS66
D	SER70
D	LEU88
D	HIS92
D	LEU96
D	ASN102
D	PHE103
D	LEU141
D	HOH164

---

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: Phosphoserine => ECO:0000250|UniProtKB:P68871

Chain	Residue	Details
B	SER44
D	SER44
A	SER49
C	SER3
C	SER35
C	SER49

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P68871

Chain	Residue	Details
B	LYS59
B	LYS82
B	LYS144
D	LYS59
D	LYS82
D	LYS144

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P68871

Chain	Residue	Details
B	CYS93
D	CYS93

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P69905

Chain	Residue	Details
A	TYR24
C	TYR24

---

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

Chain	Residue	Details
A	SER102
A	SER124
A	SER138
C	SER102
C	SER124
C	SER138

---

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

Chain	Residue	Details
A	THR108
A	THR134
A	THR137
C	THR108
C	THR134
C	THR137

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