2ZFO

Structure of the partially unliganded met state of 400 kDa hemoglobin: Insights into ligand-induced structural changes of giant hemoglobins

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005344	molecular_function	oxygen carrier activity
A	0005506	molecular_function	iron ion binding
A	0005576	cellular_component	extracellular region
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	0046872	molecular_function	metal ion binding
B	0005344	molecular_function	oxygen carrier activity
B	0005506	molecular_function	iron ion binding
B	0005576	cellular_component	extracellular region
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	0046872	molecular_function	metal ion binding
C	0005344	molecular_function	oxygen carrier activity
C	0005506	molecular_function	iron ion binding
C	0005576	cellular_component	extracellular region
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	0046872	molecular_function	metal ion binding
D	0005344	molecular_function	oxygen carrier activity
D	0005576	cellular_component	extracellular region
D	0015671	biological_process	oxygen transport
D	0019825	molecular_function	oxygen binding
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM A 200

Chain	Residue
A	LEU45
A	ILE138
A	OXY201
A	HOH1102
A	HOH1188
A	HOH1193
D	HIS91
D	GLN95
D	HOH1197
A	PHE46
A	VAL49
A	ARG65
A	HIS94
A	ARG97
A	LEU99
A	ASN103
A	TYR131

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE OXY A 201

Chain	Residue
A	PHE32
A	PHE46
A	HIS62
A	VAL66
A	HEM200

---

site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM B 200

Chain	Residue
B	LEU45
B	PHE46
B	ARG48
B	VAL49
B	ARG65
B	GLY69
B	LEU70
B	GLN93
B	HIS94
B	ILE99
B	GLY103
B	TYR104
B	PHE107
B	ILE140
B	HOH1027
B	HOH1339
C	HIS93
C	GLN97

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 501

Chain	Residue
B	GLU20
B	GLY21
B	THR22
B	ASN23
B	HOH1227
C	ASN82

---

site_id	AC5
Number of Residues	19
Details	BINDING SITE FOR RESIDUE HEM C 200

Chain	Residue
B	ARG89
B	GLN93
C	LEU49
C	PHE50
C	VAL53
C	HIS66
C	ARG69
C	VAL70
C	GLY73
C	LEU74
C	GLN97
C	HIS98
C	ARG101
C	HIS108
C	PHE109
C	MET112
C	ILE143
C	HOH1125
C	HOH1463

---

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL C 502

Chain	Residue
B	ARG122
C	ASN82
C	ASP83
C	PRO84
C	HOH1057
C	HOH1439
D	SER124
D	ALA125
D	HIS126
D	HOH1281

---

site_id	AC7
Number of Residues	18
Details	BINDING SITE FOR RESIDUE HEM D 200

Chain	Residue
A	HIS89
A	GLN93
A	HOH1049
A	HOH1193
D	MET49
D	PHE50
D	GLN64
D	ARG67
D	VAL68
D	ALA72
D	HIS96
D	ILE99
D	ALA106
D	VAL107
D	LEU110
D	ILE141
D	HOH1009
D	HOH1237

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	567
Details	Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"description":"proximal binding residue"}

Chain

Residue

Details

---