Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5XB1

human ferritin mutant - E-helix deletion

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006826	biological_process	iron ion transport
A	0006879	biological_process	intracellular iron ion homeostasis
A	0008199	molecular_function	ferric iron binding
B	0006826	biological_process	iron ion transport
B	0006879	biological_process	intracellular iron ion homeostasis
B	0008199	molecular_function	ferric iron binding
C	0006826	biological_process	iron ion transport
C	0006879	biological_process	intracellular iron ion homeostasis
C	0008199	molecular_function	ferric iron binding
D	0006826	biological_process	iron ion transport
D	0006879	biological_process	intracellular iron ion homeostasis
D	0008199	molecular_function	ferric iron binding
E	0006826	biological_process	iron ion transport
E	0006879	biological_process	intracellular iron ion homeostasis
E	0008199	molecular_function	ferric iron binding
F	0006826	biological_process	iron ion transport
F	0006879	biological_process	intracellular iron ion homeostasis
F	0008199	molecular_function	ferric iron binding
G	0006826	biological_process	iron ion transport
G	0006879	biological_process	intracellular iron ion homeostasis
G	0008199	molecular_function	ferric iron binding
H	0006826	biological_process	iron ion transport
H	0006879	biological_process	intracellular iron ion homeostasis
H	0008199	molecular_function	ferric iron binding
I	0006826	biological_process	iron ion transport
I	0006879	biological_process	intracellular iron ion homeostasis
I	0008199	molecular_function	ferric iron binding
J	0006826	biological_process	iron ion transport
J	0006879	biological_process	intracellular iron ion homeostasis
J	0008199	molecular_function	ferric iron binding
K	0006826	biological_process	iron ion transport
K	0006879	biological_process	intracellular iron ion homeostasis
K	0008199	molecular_function	ferric iron binding
L	0006826	biological_process	iron ion transport
L	0006879	biological_process	intracellular iron ion homeostasis
L	0008199	molecular_function	ferric iron binding
M	0006826	biological_process	iron ion transport
M	0006879	biological_process	intracellular iron ion homeostasis
M	0008199	molecular_function	ferric iron binding
N	0006826	biological_process	iron ion transport
N	0006879	biological_process	intracellular iron ion homeostasis
N	0008199	molecular_function	ferric iron binding
O	0006826	biological_process	iron ion transport
O	0006879	biological_process	intracellular iron ion homeostasis
O	0008199	molecular_function	ferric iron binding
P	0006826	biological_process	iron ion transport
P	0006879	biological_process	intracellular iron ion homeostasis
P	0008199	molecular_function	ferric iron binding
Q	0006826	biological_process	iron ion transport
Q	0006879	biological_process	intracellular iron ion homeostasis
Q	0008199	molecular_function	ferric iron binding
R	0006826	biological_process	iron ion transport
R	0006879	biological_process	intracellular iron ion homeostasis
R	0008199	molecular_function	ferric iron binding
S	0006826	biological_process	iron ion transport
S	0006879	biological_process	intracellular iron ion homeostasis
S	0008199	molecular_function	ferric iron binding
T	0006826	biological_process	iron ion transport
T	0006879	biological_process	intracellular iron ion homeostasis
T	0008199	molecular_function	ferric iron binding
U	0006826	biological_process	iron ion transport
U	0006879	biological_process	intracellular iron ion homeostasis
U	0008199	molecular_function	ferric iron binding
V	0006826	biological_process	iron ion transport
V	0006879	biological_process	intracellular iron ion homeostasis
V	0008199	molecular_function	ferric iron binding
W	0006826	biological_process	iron ion transport
W	0006879	biological_process	intracellular iron ion homeostasis
W	0008199	molecular_function	ferric iron binding
X	0006826	biological_process	iron ion transport
X	0006879	biological_process	intracellular iron ion homeostasis
X	0008199	molecular_function	ferric iron binding

Functional Information from PROSITE/UniProt

site_id	PS00204
Number of Residues	21
Details	FERRITIN_2 Ferritin iron-binding regions signature 2. DphLCDFIEthYLneqvkaIK

Chain	Residue	Details
A	ASP127-LYS147

site_id	PS00540
Number of Residues	19
Details	FERRITIN_1 Ferritin iron-binding regions signature 1. EeREhaEKLMklQNqRgGR

Chain	Residue	Details
A	GLU62-ARG80

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:1992356, ECO:0007744\|PDB:1FHA

Chain	Residue	Details
A	GLU28
E	HIS66
F	GLU28
F	HIS66
G	GLU28
G	HIS66
H	GLU28
H	HIS66
I	GLU28
I	HIS66
J	GLU28
A	HIS66
J	HIS66
K	GLU28
K	HIS66
L	GLU28
L	HIS66
M	GLU28
M	HIS66
N	GLU28
N	HIS66
O	GLU28
B	GLU28
O	HIS66
P	GLU28
P	HIS66
Q	GLU28
Q	HIS66
R	GLU28
R	HIS66
S	GLU28
S	HIS66
T	GLU28
B	HIS66
T	HIS66
U	GLU28
U	HIS66
V	GLU28
V	HIS66
W	GLU28
W	HIS66
X	GLU28
X	HIS66
C	GLU28
C	HIS66
D	GLU28
D	HIS66
E	GLU28

site_id	SWS_FT_FI2
Number of Residues	72
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00085

Chain	Residue	Details
A	GLU63
D	GLU63
D	GLU108
D	GLN142
E	GLU63
E	GLU108
E	GLN142
F	GLU63
F	GLU108
F	GLN142
G	GLU63
A	GLU108
G	GLU108
G	GLN142
H	GLU63
H	GLU108
H	GLN142
I	GLU63
I	GLU108
I	GLN142
J	GLU63
J	GLU108
A	GLN142
J	GLN142
K	GLU63
K	GLU108
K	GLN142
L	GLU63
L	GLU108
L	GLN142
M	GLU63
M	GLU108
M	GLN142
B	GLU63
N	GLU63
N	GLU108
N	GLN142
O	GLU63
O	GLU108
O	GLN142
P	GLU63
P	GLU108
P	GLN142
Q	GLU63
B	GLU108
Q	GLU108
Q	GLN142
R	GLU63
R	GLU108
R	GLN142
S	GLU63
S	GLU108
S	GLN142
T	GLU63
T	GLU108
B	GLN142
T	GLN142
U	GLU63
U	GLU108
U	GLN142
V	GLU63
V	GLU108
V	GLN142
W	GLU63
W	GLU108
W	GLN142
C	GLU63
X	GLU63
X	GLU108
X	GLN142
C	GLU108
C	GLN142

site_id	SWS_FT_FI3
Number of Residues	24
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	MET1
J	MET1
K	MET1
L	MET1
M	MET1
N	MET1
O	MET1
P	MET1
Q	MET1
R	MET1
S	MET1
B	MET1
T	MET1
U	MET1
V	MET1
W	MET1
X	MET1
C	MET1
D	MET1
E	MET1
F	MET1
G	MET1
H	MET1
I	MET1

site_id	SWS_FT_FI4
Number of Residues	24
Details	MOD_RES: N-acetylthreonine; in Ferritin heavy chain, N-terminally processed => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	THR2
J	THR2
K	THR2
L	THR2
M	THR2
N	THR2
O	THR2
P	THR2
Q	THR2
R	THR2
S	THR2
B	THR2
T	THR2
U	THR2
V	THR2
W	THR2
X	THR2
C	THR2
D	THR2
E	THR2
F	THR2
G	THR2
H	THR2
I	THR2

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)