Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2GTL

Lumbricus Erythrocruorin at 3.5A 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	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	0005506	molecular_function	iron ion binding
D	0005576	cellular_component	extracellular region
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	0046872	molecular_function	metal ion binding
E	0005344	molecular_function	oxygen carrier activity
E	0005506	molecular_function	iron ion binding
E	0005576	cellular_component	extracellular region
E	0005833	cellular_component	hemoglobin complex
E	0015671	biological_process	oxygen transport
E	0019825	molecular_function	oxygen binding
E	0020037	molecular_function	heme binding
E	0046872	molecular_function	metal ion binding
F	0005344	molecular_function	oxygen carrier activity
F	0005506	molecular_function	iron ion binding
F	0005576	cellular_component	extracellular region
F	0005833	cellular_component	hemoglobin complex
F	0015671	biological_process	oxygen transport
F	0019825	molecular_function	oxygen binding
F	0020037	molecular_function	heme binding
F	0046872	molecular_function	metal ion binding
G	0005344	molecular_function	oxygen carrier activity
G	0005506	molecular_function	iron ion binding
G	0005576	cellular_component	extracellular region
G	0005833	cellular_component	hemoglobin complex
G	0015671	biological_process	oxygen transport
G	0019825	molecular_function	oxygen binding
G	0020037	molecular_function	heme binding
G	0046872	molecular_function	metal ion binding
H	0005344	molecular_function	oxygen carrier activity
H	0005506	molecular_function	iron ion binding
H	0005576	cellular_component	extracellular region
H	0005833	cellular_component	hemoglobin complex
H	0015671	biological_process	oxygen transport
H	0019825	molecular_function	oxygen binding
H	0020037	molecular_function	heme binding
H	0046872	molecular_function	metal ion binding
I	0005344	molecular_function	oxygen carrier activity
I	0005506	molecular_function	iron ion binding
I	0005576	cellular_component	extracellular region
I	0005833	cellular_component	hemoglobin complex
I	0015671	biological_process	oxygen transport
I	0019825	molecular_function	oxygen binding
I	0020037	molecular_function	heme binding
I	0046872	molecular_function	metal ion binding
J	0005344	molecular_function	oxygen carrier activity
J	0005506	molecular_function	iron ion binding
J	0005576	cellular_component	extracellular region
J	0005833	cellular_component	hemoglobin complex
J	0015671	biological_process	oxygen transport
J	0019825	molecular_function	oxygen binding
J	0020037	molecular_function	heme binding
J	0046872	molecular_function	metal ion binding
K	0005344	molecular_function	oxygen carrier activity
K	0005506	molecular_function	iron ion binding
K	0005576	cellular_component	extracellular region
K	0005833	cellular_component	hemoglobin complex
K	0015671	biological_process	oxygen transport
K	0019825	molecular_function	oxygen binding
K	0020037	molecular_function	heme binding
K	0046872	molecular_function	metal ion binding
L	0005344	molecular_function	oxygen carrier activity
L	0005506	molecular_function	iron ion binding
L	0005576	cellular_component	extracellular region
L	0005833	cellular_component	hemoglobin complex
L	0015671	biological_process	oxygen transport
L	0019825	molecular_function	oxygen binding
L	0020037	molecular_function	heme binding
L	0046872	molecular_function	metal ion binding
M	0046872	molecular_function	metal ion binding
O	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA M 250

Chain	Residue
M	LEU81
M	ASP84
M	GLU86
M	ASP88
M	ASP94
M	GLU95

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA M 251

Chain	Residue
G	GLU9
G	ASP86
M	ASP122

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN M 252

Chain	Residue
N	ARG123
N	SER153
N	SER164
N	HIS190
N	ARG209

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA N 250

Chain	Residue
N	LEU81
N	ASP84
N	HIS86
N	ASP88
N	ASP94
N	GLU95

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA O 250

Chain	Residue
O	PHE81
O	ASP84
O	HIS86
O	ASP88
O	ASP94
O	GLU95

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO A 161

Chain	Residue
A	PHE39
A	PHE53
A	HIS69
A	VAL73
A	HEM160

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO B 161

Chain	Residue
B	TRP34
B	PHE48
B	HIS64
B	VAL68
B	HEM160

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CMO C 161

Chain	Residue
C	PHE54
C	HIS70
C	ILE74
C	HEM160

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO D 161

Chain	Residue
D	TRP39
D	PHE53
D	HIS69
D	VAL73
D	HEM160

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO E 161

Chain	Residue
E	PHE39
E	PHE53
E	HIS69
E	VAL73
E	HEM160

site_id	BC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO F 161

Chain	Residue
F	TRP34
F	PHE48
F	HIS64
F	VAL68
F	HEM160

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CMO G 161

Chain	Residue
G	PHE54
G	HIS70
G	ILE74
G	HEM160

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO H 161

Chain	Residue
H	TRP39
H	PHE53
H	HIS69
H	VAL73
H	HEM160

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO I 161

Chain	Residue
I	PHE39
I	PHE53
I	HIS69
I	VAL73
I	HEM160

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO J 161

Chain	Residue
J	TRP34
J	PHE48
J	HIS64
J	VAL68
J	HEM160

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CMO K 161

Chain	Residue
K	PHE54
K	HIS70
K	ILE74
K	HEM160

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CMO L 161

Chain	Residue
L	TRP39
L	PHE53
L	HIS69
L	VAL73
L	HEM160

site_id	BC9
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM A 160

Chain	Residue
A	PHE53
A	ARG55
A	VAL56
A	HIS69
A	ARG72
A	HIS101
A	ARG104
A	TYR111
A	PHE112
A	PHE139
A	CMO161
D	HIS96

site_id	CC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM B 160

Chain	Residue
B	GLN95
B	HIS96
B	ARG99
B	ILE101
B	TYR105
B	PHE106
B	PHE109
B	ILE141
B	CMO161
C	HIS97
C	GLN101
B	LEU47
B	PHE48
B	ARG50
B	VAL68

site_id	CC2
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM C 160

Chain	Residue
B	HIS91
C	PHE54
C	ARG56
C	VAL57
C	HIS70
C	ARG73
C	LEU78
C	GLN101
C	HIS102
C	ARG105
C	HIS112
C	PHE113
C	PHE116
C	LEU144
C	CMO161

site_id	CC3
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM D 160

Chain	Residue
A	HIS96
A	GLN100
D	PRO52
D	PHE53
D	ARG55
D	GLN100
D	HIS101
D	ARG104
D	PHE110
D	PHE111
D	PHE114
D	CMO161

site_id	CC4
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM E 160

Chain	Residue
E	PHE53
E	ARG55
E	VAL56
E	ARG72
E	HIS101
E	ARG104
E	TYR111
E	PHE112
E	PHE139
E	CMO161
H	HIS96

site_id	CC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM F 160

Chain	Residue
F	LEU47
F	PHE48
F	ARG50
F	VAL68
F	GLN95
F	HIS96
F	ARG99
F	ILE101
F	TYR105
F	PHE106
F	PHE109
F	ILE141
F	CMO161
G	HIS97
G	GLN101

site_id	CC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE HEM G 160

Chain	Residue
F	HIS91
G	PHE54
G	ARG56
G	VAL57
G	HIS70
G	ARG73
G	LEU78
G	GLN101
G	HIS102
G	ARG105
G	VAL108
G	HIS112
G	PHE113
G	PHE116
G	LEU144
G	CMO161

site_id	CC7
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM H 160

Chain	Residue
E	HIS96
E	GLN100
H	PHE53
H	ARG55
H	GLN100
H	HIS101
H	ARG104
H	PHE110
H	PHE111
H	PHE114
H	CMO161

site_id	CC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE HEM I 160

Chain	Residue
I	PHE53
I	ARG55
I	VAL56
I	HIS69
I	HIS101
I	ARG104
I	TYR111
I	PHE112
I	PHE139
I	CMO161
L	HIS96

site_id	CC9
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM J 160

Chain	Residue
J	LEU47
J	PHE48
J	ARG50
J	VAL68
J	GLN95
J	HIS96
J	ARG99
J	ILE101
J	TYR105
J	PHE106
J	PHE109
J	ILE141
J	CMO161
K	HIS97
K	GLN101

site_id	DC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE HEM K 160

Chain	Residue
J	HIS91
K	PHE54
K	ARG56
K	VAL57
K	HIS70
K	ARG73
K	LEU78
K	GLN101
K	HIS102
K	ARG105
K	HIS112
K	PHE113
K	PHE116
K	LEU144
K	CMO161

site_id	DC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM L 160

Chain	Residue
I	HIS96
I	GLN100
L	PRO52
L	PHE53
L	ARG55
L	GLN100
L	HIS101
L	ARG104
L	PHE110
L	PHE111
L	PHE114
L	CMO161

Functional Information from PROSITE/UniProt

site_id	PS01209
Number of Residues	25
Details	LDLRA_1 LDL-receptor class A (LDLRA) domain signature. CIhdllf.CDgekDCrdgsDEDpet..C

Chain	Residue	Details
M	CYS76-CYS100
N	CYS76-CYS100
O	CYS76-CYS98

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	861
Details	Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	9
Details	Binding site: {"description":"proximal binding residue"}

Chain

Residue

Details

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