3NG6

The crystal structure of hemoglobin I from Trematomus newnesi in deoxygenated state obtained through an oxidation/reduction cycle in which potassium hexacyanoferrate and sodium dithionite were alternatively added

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	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	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	0072562	cellular_component	blood microparticle
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	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	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	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	0072562	cellular_component	blood microparticle
D	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM A 200

Chain	Residue
A	TYR42
A	VAL94
A	ASN98
A	LEU102
A	LEU137
A	PHE43
A	HIS59
A	LYS62
A	VAL63
A	ILE67
A	GLN87
A	HIS88
A	LEU92

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM B 400

Chain	Residue
B	TYR41
B	HIS63
B	LYS66
B	VAL67
B	LEU88
B	HIS92
B	LEU96
B	ASN102
B	PHE103
B	LEU106
B	LEU141

---

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM C 600

Chain	Residue
C	MET32
C	TYR42
C	PHE43
C	TRP46
C	HIS59
C	LYS62
C	VAL63
C	GLY66
C	ILE67
C	LEU84
C	GLN87
C	HIS88
C	LEU92
C	LEU102

---

site_id	AC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM D 800

Chain	Residue
D	THR38
D	TYR41
D	PHE42
D	HIS63
D	VAL67
D	HIS92
D	LEU96
D	ASN102
D	PHE103
D	LEU106
D	LEU141

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: distal binding residue => ECO:0000269|PubMed:12093902, ECO:0007744|PDB:1LA6

Chain	Residue	Details
B	HIS63
D	HIS63

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: proximal binding residue => ECO:0000269|PubMed:12093902, ECO:0007744|PDB:1LA6, ECO:0007744|PDB:1T1N, ECO:0007744|PDB:3D1K, ECO:0007744|PDB:3NFE, ECO:0007744|PDB:3NG6

Chain	Residue	Details
B	HIS92
D	HIS92

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N-acetylserine => ECO:0000269|PubMed:8144556

Chain	Residue	Details
A	SER1
C	SER1

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