Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2OIF

The crystal structure of ferric cyanide bound barley hexacoordinate hemoglobin.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0016491	molecular_function	oxidoreductase activity
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0046872	molecular_function	metal ion binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0016491	molecular_function	oxidoreductase activity
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0046872	molecular_function	metal ion binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0016491	molecular_function	oxidoreductase activity
C	0019825	molecular_function	oxygen binding
C	0020037	molecular_function	heme binding
C	0046872	molecular_function	metal ion binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0016491	molecular_function	oxidoreductase activity
D	0019825	molecular_function	oxygen binding
D	0020037	molecular_function	heme binding
D	0046872	molecular_function	metal ion binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0016491	molecular_function	oxidoreductase activity
E	0019825	molecular_function	oxygen binding
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0016491	molecular_function	oxidoreductase activity
F	0019825	molecular_function	oxygen binding
F	0020037	molecular_function	heme binding
F	0046872	molecular_function	metal ion binding
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0016491	molecular_function	oxidoreductase activity
G	0019825	molecular_function	oxygen binding
G	0020037	molecular_function	heme binding
G	0046872	molecular_function	metal ion binding
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0016491	molecular_function	oxidoreductase activity
H	0019825	molecular_function	oxygen binding
H	0020037	molecular_function	heme binding
H	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CYN A 201

Chain	Residue
A	PHE37
A	PHE51
A	HIS70
A	VAL74
A	HEM163

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CYN B 202

Chain	Residue
B	PHE37
B	HIS70
B	VAL74
B	HEM163

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CYN C 203

Chain	Residue
C	PHE37
C	PHE51
C	HIS70
C	VAL74
C	HEM163

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CYN D 204

Chain	Residue
D	PHE37
D	PHE51
D	HIS70
D	HEM163

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CYN E 205

Chain	Residue
E	PHE37
E	HIS70
E	VAL74
E	HEM163

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CYN F 206

Chain	Residue
F	PHE37
F	PHE51
F	HIS70
F	VAL74
F	HEM163

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CYN G 207

Chain	Residue
G	PHE37
G	PHE51
G	HIS70
G	VAL74
G	HEM163

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CYN H 208

Chain	Residue
H	PHE37
H	PHE51
H	HIS70
H	VAL74
H	HEM163

site_id	AC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM A 163

Chain	Residue
A	MET50
A	PHE51
A	VAL74
A	MET77
A	LEU101
A	HIS105
A	VAL110
A	HIS114
A	PHE115
A	THR118
A	LEU150
A	CYN201

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGO A 1210

Chain	Residue
A	GLY113
A	PGO1215
F	HIS114

site_id	BC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGO A 1211

Chain	Residue
A	LYS127
A	TRP135
A	ARG140

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PGO A 1215

Chain	Residue
A	HIS114
A	PGO1210

site_id	BC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM B 163

Chain	Residue
B	MET50
B	PHE51
B	PRO52
B	PHE53
B	VAL74
B	MET77
B	HIS105
B	TYR108
B	VAL110
B	PHE115
B	THR118
B	TYR147
B	LEU150
B	CYN202

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGO B 1217

Chain	Residue
B	LYS127
B	TRP135
B	ARG140
B	HOH1321

site_id	BC6
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM C 163

Chain	Residue
C	MET50
C	PHE51
C	PRO52
C	MET77
C	LEU101
C	HIS105
C	VAL110
C	HIS114
C	PHE115
C	THR118
C	TYR147
C	LEU150
C	CYN203
C	HOH706

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGO C 1218

Chain	Residue
C	LYS127
C	TRP135
C	ARG140

site_id	BC8
Number of Residues	17
Details	BINDING SITE FOR RESIDUE HEM D 163

Chain	Residue
D	HIS105
D	TYR108
D	VAL110
D	HIS114
D	PHE115
D	THR118
D	TYR147
D	LEU150
D	CYN204
D	HOH1239
D	MET50
D	PHE51
D	PRO52
D	PHE53
D	VAL74
D	MET77
D	LEU101

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PGO D 1209

Chain	Residue
B	GLY113
D	HOH1320

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PGO D 1219

Chain	Residue
B	HOH1268
D	LYS127
D	TRP135
D	ARG140
D	HOH1255
D	HOH1257
D	HOH1274

site_id	CC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM E 163

Chain	Residue
E	MET50
E	PHE51
E	PRO52
E	PHE53
E	MET77
E	LEU101
E	HIS105
E	TYR108
E	VAL110
E	HIS114
E	PHE115
E	THR118
E	LEU150
E	CYN205

site_id	CC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PGO E 1212

Chain	Residue
C	GLY113

site_id	CC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGO E 1216

Chain	Residue
E	LYS127
E	TRP135
E	ARG140
E	HOH827

site_id	CC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM F 163

Chain	Residue
F	MET50
F	PHE51
F	VAL74
F	MET77
F	LEU101
F	HIS105
F	TYR108
F	VAL110
F	HIS114
F	PHE115
F	THR118
F	TYR147
F	LEU150
F	CYN206

site_id	CC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGO F 1220

Chain	Residue
F	LYS127
F	TRP135
F	ARG140
F	HOH344

site_id	CC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM G 163

Chain	Residue
G	MET50
G	PHE51
G	PRO52
G	MET77
G	LEU101
G	HIS105
G	TYR108
G	VAL110
G	HIS114
G	PHE115
G	THR118
G	TYR147
G	LEU150
G	CYN207

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGO G 1214

Chain	Residue
G	TRP135
G	PRO137
G	ARG140

site_id	CC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM H 163

Chain	Residue
H	MET50
H	PHE51
H	PRO52
H	MET77
H	THR78
H	LEU101
H	HIS105
H	TYR108
H	VAL110
H	HIS114
H	THR118
H	TYR147
H	LEU150
H	CYN208

site_id	DC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PGO H 1213

Chain	Residue
H	HIS114

site_id	DC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PGO H 1221

Chain	Residue
H	LYS127
H	TRP135
H	ARG140
H	HOH1319

Functional Information from PROSITE/UniProt

site_id	PS00208
Number of Residues	12
Details	PLANT_GLOBIN Plant hemoglobins signature. NPkLktHAvsvF

Chain	Residue	Details
A	ASN64-PHE75

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:O04986

Chain	Residue	Details
A	LYS66
D	LYS66
D	ARG100
D	THR104
E	LYS66
E	ARG100
E	THR104
F	LYS66
F	ARG100
F	THR104
G	LYS66
A	ARG100
G	ARG100
G	THR104
H	LYS66
H	ARG100
H	THR104
A	THR104
B	LYS66
B	ARG100
B	THR104
C	LYS66
C	ARG100
C	THR104

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: distal binding residue => ECO:0000255\|PROSITE-ProRule:PRU00238

Chain	Residue	Details
A	HIS70
B	HIS70
C	HIS70
D	HIS70
E	HIS70
F	HIS70
G	HIS70
H	HIS70

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: proximal binding residue => ECO:0000255\|PROSITE-ProRule:PRU00238, ECO:0000269\|PubMed:17560601, ECO:0007744\|PDB:2OIF

Chain	Residue	Details
A	HIS105
B	HIS105
C	HIS105
D	HIS105
E	HIS105
F	HIS105
G	HIS105
H	HIS105

site_id	SWS_FT_FI4
Number of Residues	8
Details	SITE: Homodimerization => ECO:0000269\|PubMed:17560601, ECO:0007744\|PDB:2OIF

Chain	Residue	Details
A	ARG140
B	ARG140
C	ARG140
D	ARG140
E	ARG140
F	ARG140
G	ARG140
H	ARG140

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)