Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3LHB

THE 2.7 ANGSTROM CRYSTAL STRUCTURE OF DEOXYGENATED HEMOGLOBIN FROM THE SEA LAMPREY (PETROMYZON MARINUS)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005344	molecular_function	oxygen carrier activity
A	0005506	molecular_function	iron ion binding
A	0015671	biological_process	oxygen transport
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	0005344	molecular_function	oxygen carrier activity
B	0005506	molecular_function	iron ion binding
B	0015671	biological_process	oxygen transport
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	0005344	molecular_function	oxygen carrier activity
C	0005506	molecular_function	iron ion binding
C	0015671	biological_process	oxygen transport
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	0005344	molecular_function	oxygen carrier activity
D	0005506	molecular_function	iron ion binding
D	0015671	biological_process	oxygen transport
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	0005344	molecular_function	oxygen carrier activity
E	0005506	molecular_function	iron ion binding
E	0015671	biological_process	oxygen transport
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	0005344	molecular_function	oxygen carrier activity
F	0005506	molecular_function	iron ion binding
F	0015671	biological_process	oxygen transport
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	0005344	molecular_function	oxygen carrier activity
G	0005506	molecular_function	iron ion binding
G	0015671	biological_process	oxygen transport
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	0005344	molecular_function	oxygen carrier activity
H	0005506	molecular_function	iron ion binding
H	0015671	biological_process	oxygen transport
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
I	0005344	molecular_function	oxygen carrier activity
I	0005506	molecular_function	iron ion binding
I	0015671	biological_process	oxygen transport
I	0016491	molecular_function	oxidoreductase activity
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	0015671	biological_process	oxygen transport
J	0016491	molecular_function	oxidoreductase activity
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	0015671	biological_process	oxygen transport
K	0016491	molecular_function	oxidoreductase activity
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	0015671	biological_process	oxygen transport
L	0016491	molecular_function	oxidoreductase activity
L	0019825	molecular_function	oxygen binding
L	0020037	molecular_function	heme binding
L	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM A 150

Chain	Residue
A	PHE51
A	PHE52
A	LYS54
A	HIS73
A	ARG76
A	LYS104
A	HIS105
A	PHE109
A	VAL111
A	TYR115
A	PHE116
A	LEU119
A	LEU145

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM B 150

Chain	Residue
B	PHE51
B	PHE52
B	LYS54
B	HIS73
B	ARG76
B	ALA80
B	LYS104
B	HIS105
B	PHE109
B	VAL111
B	TYR115
B	PHE116
B	LEU119
B	LEU145

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM C 150

Chain	Residue
C	PHE51
C	PHE52
C	LYS54
C	HIS73
C	ARG76
C	ALA80
C	LYS104
C	HIS105
C	PHE109
C	VAL111
C	TYR115
C	PHE116
C	LEU119
C	LEU145

site_id	AC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM D 150

Chain	Residue
D	PHE51
D	PHE52
D	LYS54
D	HIS73
D	ARG76
D	LYS104
D	HIS105
D	PHE109
D	VAL111
D	TYR115
D	PHE116
D	LEU119
D	LEU145

site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM E 150

Chain	Residue
E	PHE51
E	PHE52
E	LYS54
E	HIS73
E	ARG76
E	ALA80
E	LYS104
E	HIS105
E	PHE109
E	VAL111
E	TYR115
E	PHE116
E	LEU119
E	LEU145

site_id	AC6
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM F 150

Chain	Residue
F	PHE109
F	VAL111
F	TYR115
F	PHE116
F	LEU119
F	LEU145
F	PHE51
F	PHE52
F	LYS54
F	HIS73
F	ARG76
F	LYS104
F	HIS105

site_id	AC7
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM G 150

Chain	Residue
G	PHE51
G	PHE52
G	LYS54
G	HIS73
G	ARG76
G	LYS104
G	HIS105
G	PHE109
G	VAL111
G	TYR115
G	PHE116
G	LEU119
G	LEU145

site_id	AC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE HEM H 150

Chain	Residue
H	PHE51
H	PHE52
H	LYS54
H	HIS73
H	ARG76
H	LYS104
H	HIS105
H	PHE109
H	VAL111
H	TYR115
H	LEU119
H	LEU145

site_id	AC9
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM I 150

Chain	Residue
I	PHE51
I	PHE52
I	LYS54
I	HIS73
I	ARG76
I	ALA80
I	LYS104
I	HIS105
I	PHE109
I	VAL111
I	TYR115
I	PHE116
I	LEU119
I	LEU145

site_id	BC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM J 150

Chain	Residue
J	PHE51
J	PHE52
J	LYS54
J	HIS73
J	ARG76
J	LYS104
J	HIS105
J	PHE109
J	VAL111
J	TYR115
J	PHE116
J	LEU119
J	LEU145

site_id	BC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE HEM K 150

Chain	Residue
K	PHE51
K	PHE52
K	LYS54
K	HIS73
K	ARG76
K	ALA80
K	LYS104
K	HIS105
K	PHE109
K	VAL111
K	TYR115
K	PHE116
K	LEU119
K	LEU145

site_id	BC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE HEM L 150

Chain	Residue
L	PHE51
L	PHE52
L	LYS54
L	HIS73
L	ARG76
L	LYS104
L	HIS105
L	PHE109
L	VAL111
L	TYR115
L	PHE116
L	LEU119
L	LEU145

site_id	F10
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
J	HIS73
J	HIS105

site_id	F11
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
K	HIS73
K	HIS105

site_id	F12
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
L	HIS73
L	HIS105

site_id	FE1
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
A	HIS73
A	HIS105

site_id	FE2
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
B	HIS73
B	HIS105

site_id	FE3
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
C	HIS73
C	HIS105

site_id	FE4
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
D	HIS73
D	HIS105

site_id	FE5
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
E	HIS105
E	HIS73

site_id	FE6
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
F	HIS73
F	HIS105

site_id	FE7
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
G	HIS73
G	HIS105

site_id	FE8
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
H	HIS73
H	HIS105

site_id	FE9
Number of Residues	2
Details	HIS 73 IS THE PROXIMAL HISTIDINE AND HIS 105 IS THE DISTAL HISTIDINE

Chain	Residue
I	HIS73
I	HIS105

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1668
Details	Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"description":"distal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4032476","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	12
Details	Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4032476","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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