Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4F1E

The Crystal Structure of a Human MitoNEET mutant with Asp 67 replaced by a Gly

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0010506	biological_process	regulation of autophagy
A	0043231	cellular_component	intracellular membrane-bounded organelle
A	0051537	molecular_function	2 iron, 2 sulfur cluster binding
B	0010506	biological_process	regulation of autophagy
B	0043231	cellular_component	intracellular membrane-bounded organelle
B	0051537	molecular_function	2 iron, 2 sulfur cluster binding
C	0010506	biological_process	regulation of autophagy
C	0043231	cellular_component	intracellular membrane-bounded organelle
C	0051537	molecular_function	2 iron, 2 sulfur cluster binding
D	0010506	biological_process	regulation of autophagy
D	0043231	cellular_component	intracellular membrane-bounded organelle
D	0051537	molecular_function	2 iron, 2 sulfur cluster binding
E	0010506	biological_process	regulation of autophagy
E	0043231	cellular_component	intracellular membrane-bounded organelle
E	0051537	molecular_function	2 iron, 2 sulfur cluster binding
F	0010506	biological_process	regulation of autophagy
F	0043231	cellular_component	intracellular membrane-bounded organelle
F	0051537	molecular_function	2 iron, 2 sulfur cluster binding
G	0010506	biological_process	regulation of autophagy
G	0043231	cellular_component	intracellular membrane-bounded organelle
G	0051537	molecular_function	2 iron, 2 sulfur cluster binding
H	0010506	biological_process	regulation of autophagy
H	0043231	cellular_component	intracellular membrane-bounded organelle
H	0051537	molecular_function	2 iron, 2 sulfur cluster binding
I	0010506	biological_process	regulation of autophagy
I	0043231	cellular_component	intracellular membrane-bounded organelle
I	0051537	molecular_function	2 iron, 2 sulfur cluster binding
J	0010506	biological_process	regulation of autophagy
J	0043231	cellular_component	intracellular membrane-bounded organelle
J	0051537	molecular_function	2 iron, 2 sulfur cluster binding
K	0010506	biological_process	regulation of autophagy
K	0043231	cellular_component	intracellular membrane-bounded organelle
K	0051537	molecular_function	2 iron, 2 sulfur cluster binding
L	0010506	biological_process	regulation of autophagy
L	0043231	cellular_component	intracellular membrane-bounded organelle
L	0051537	molecular_function	2 iron, 2 sulfur cluster binding
M	0010506	biological_process	regulation of autophagy
M	0043231	cellular_component	intracellular membrane-bounded organelle
M	0051537	molecular_function	2 iron, 2 sulfur cluster binding
N	0010506	biological_process	regulation of autophagy
N	0043231	cellular_component	intracellular membrane-bounded organelle
N	0051537	molecular_function	2 iron, 2 sulfur cluster binding
O	0010506	biological_process	regulation of autophagy
O	0043231	cellular_component	intracellular membrane-bounded organelle
O	0051537	molecular_function	2 iron, 2 sulfur cluster binding
P	0010506	biological_process	regulation of autophagy
P	0043231	cellular_component	intracellular membrane-bounded organelle
P	0051537	molecular_function	2 iron, 2 sulfur cluster binding
Q	0010506	biological_process	regulation of autophagy
Q	0043231	cellular_component	intracellular membrane-bounded organelle
Q	0051537	molecular_function	2 iron, 2 sulfur cluster binding
R	0010506	biological_process	regulation of autophagy
R	0043231	cellular_component	intracellular membrane-bounded organelle
R	0051537	molecular_function	2 iron, 2 sulfur cluster binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES A 201

Chain	Residue
A	CYS72
A	ARG73
A	CYS74
A	CYS83
A	ASP84
A	ALA86
A	HIS87
A	PRO100

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES B 201

Chain	Residue
B	ARG73
B	CYS74
B	CYS83
B	ASP84
B	ALA86
B	HIS87
B	CYS72

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES C 201

Chain	Residue
C	CYS72
C	ARG73
C	CYS74
C	SER77
C	CYS83
C	ASP84
C	ALA86
C	HIS87

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES D 500

Chain	Residue
D	CYS72
D	ARG73
D	CYS74
D	SER77
D	CYS83
D	ASP84
D	ALA86
D	HIS87

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES E 201

Chain	Residue
E	CYS72
E	ARG73
E	CYS74
E	CYS83
E	ASP84
E	GLY85
E	ALA86
E	HIS87

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES F 201

Chain	Residue
F	CYS72
F	ARG73
F	CYS74
F	CYS83
F	ASP84
F	ALA86
F	HIS87

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES G 201

Chain	Residue
G	CYS72
G	ARG73
G	CYS74
G	CYS83
G	ASP84
G	GLY85
G	ALA86
G	HIS87

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES H 201

Chain	Residue
H	CYS72
H	ARG73
H	CYS74
H	SER77
H	CYS83
H	ASP84
H	ALA86
H	HIS87

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES I 201

Chain	Residue
I	CYS72
I	ARG73
I	CYS74
I	CYS83
I	ASP84
I	GLY85
I	ALA86
I	HIS87

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES J 201

Chain	Residue
J	CYS72
J	ARG73
J	CYS74
J	CYS83
J	ASP84
J	GLY85
J	ALA86
J	HIS87

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES K 201

Chain	Residue
K	CYS72
K	ARG73
K	CYS74
K	CYS83
K	ASP84
K	GLY85
K	ALA86
K	HIS87

site_id	BC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES L 201

Chain	Residue
L	CYS72
L	ARG73
L	CYS74
L	CYS83
L	ASP84
L	GLY85
L	ALA86
L	HIS87

site_id	BC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE FES M 201

Chain	Residue
M	ASP84
M	GLY85
M	ALA86
M	HIS87
M	CYS72
M	ARG73
M	CYS74
M	SER77
M	CYS83

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES N 201

Chain	Residue
N	CYS72
N	ARG73
N	CYS74
N	CYS83
N	ASP84
N	ALA86
N	HIS87

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES O 201

Chain	Residue
O	CYS72
O	ARG73
O	CYS74
O	CYS83
O	ASP84
O	ALA86
O	HIS87

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES P 201

Chain	Residue
P	CYS72
P	ARG73
P	CYS74
P	SER77
P	CYS83
P	ASP84
P	ALA86
P	HIS87

site_id	BC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE FES Q 201

Chain	Residue
Q	CYS72
Q	ARG73
Q	CYS74
Q	CYS83
Q	ASP84
Q	ALA86
Q	HIS87

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE FES R 201

Chain	Residue
R	CYS72
R	ARG73
R	CYS74
R	SER77
R	CYS83
R	ASP84
R	ALA86
R	HIS87

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	ACT_SITE: Schiff-base intermediate with pyridoxal 5'-phosphate => ECO:0000269\|PubMed:36194135

Chain	Residue	Details
A	LYS55
J	LYS55
K	LYS55
L	LYS55
M	LYS55
N	LYS55
O	LYS55
P	LYS55
Q	LYS55
R	LYS55
B	LYS55
C	LYS55
D	LYS55
E	LYS55
F	LYS55
G	LYS55
H	LYS55
I	LYS55

site_id	SWS_FT_FI2
Number of Residues	72
Details	BINDING: BINDING => ECO:0000269\|PubMed:17766439, ECO:0000269\|PubMed:17766440, ECO:0000269\|PubMed:17905743, ECO:0007744\|PDB:2QD0, ECO:0007744\|PDB:2QH7, ECO:0007744\|PDB:2R13

Chain	Residue	Details
A	CYS72
C	CYS74
C	CYS83
C	HIS87
D	CYS72
D	CYS74
D	CYS83
D	HIS87
E	CYS72
E	CYS74
E	CYS83
A	CYS74
E	HIS87
F	CYS72
F	CYS74
F	CYS83
F	HIS87
G	CYS72
G	CYS74
G	CYS83
G	HIS87
H	CYS72
A	CYS83
H	CYS74
H	CYS83
H	HIS87
I	CYS72
I	CYS74
I	CYS83
I	HIS87
J	CYS72
J	CYS74
J	CYS83
A	HIS87
J	HIS87
K	CYS72
K	CYS74
K	CYS83
K	HIS87
L	CYS72
L	CYS74
L	CYS83
L	HIS87
M	CYS72
B	CYS72
M	CYS74
M	CYS83
M	HIS87
N	CYS72
N	CYS74
N	CYS83
N	HIS87
O	CYS72
O	CYS74
O	CYS83
B	CYS74
O	HIS87
P	CYS72
P	CYS74
P	CYS83
P	HIS87
Q	CYS72
Q	CYS74
Q	CYS83
Q	HIS87
R	CYS72
B	CYS83
R	CYS74
R	CYS83
R	HIS87
B	HIS87
C	CYS72

site_id	SWS_FT_FI3
Number of Residues	54
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250\|UniProtKB:Q91WS0

Chain	Residue	Details
A	LYS55
D	LYS55
D	LYS68
D	LYS104
E	LYS55
E	LYS68
E	LYS104
F	LYS55
F	LYS68
F	LYS104
G	LYS55
A	LYS68
G	LYS68
G	LYS104
H	LYS55
H	LYS68
H	LYS104
I	LYS55
I	LYS68
I	LYS104
J	LYS55
J	LYS68
A	LYS104
J	LYS104
K	LYS55
K	LYS68
K	LYS104
L	LYS55
L	LYS68
L	LYS104
M	LYS55
M	LYS68
M	LYS104
B	LYS55
N	LYS55
N	LYS68
N	LYS104
O	LYS55
O	LYS68
O	LYS104
P	LYS55
P	LYS68
P	LYS104
Q	LYS55
B	LYS68
Q	LYS68
Q	LYS104
R	LYS55
R	LYS68
R	LYS104
B	LYS104
C	LYS55
C	LYS68
C	LYS104

site_id	SWS_FT_FI4
Number of Residues	126
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:25621951

Chain	Residue	Details
A	LYS42
B	LYS78
O	LYS78
O	LYS79
O	LYS89
O	LYS105
O	LYS106
P	LYS42
P	LYS78
P	LYS79
B	LYS79
P	LYS89
P	LYS105
P	LYS106
Q	LYS42
Q	LYS78
Q	LYS79
Q	LYS89
Q	LYS105
Q	LYS106
B	LYS89
R	LYS42
R	LYS78
R	LYS79
R	LYS89
R	LYS105
R	LYS106
B	LYS105
B	LYS106
C	LYS42
C	LYS78
C	LYS79
C	LYS89
C	LYS105
C	LYS106
D	LYS42
D	LYS78
D	LYS79
D	LYS89
D	LYS105
D	LYS106
E	LYS42
A	LYS78
E	LYS78
E	LYS79
E	LYS89
E	LYS105
E	LYS106
F	LYS42
F	LYS78
F	LYS79
A	LYS79
F	LYS89
F	LYS105
F	LYS106
G	LYS42
G	LYS78
G	LYS79
G	LYS89
G	LYS105
G	LYS106
A	LYS89
H	LYS42
H	LYS78
H	LYS79
H	LYS89
H	LYS105
H	LYS106
I	LYS42
I	LYS78
A	LYS105
I	LYS79
I	LYS89
I	LYS105
I	LYS106
J	LYS42
J	LYS78
J	LYS79
J	LYS89
J	LYS105
A	LYS106
J	LYS106
K	LYS42
K	LYS78
K	LYS79
K	LYS89
K	LYS105
K	LYS106
L	LYS42
B	LYS42
L	LYS78
L	LYS79
L	LYS89
L	LYS105
L	LYS106
M	LYS42
M	LYS78
M	LYS79
M	LYS89
M	LYS105
M	LYS106
N	LYS42
N	LYS78
N	LYS79
N	LYS89
N	LYS105
N	LYS106
O	LYS42

site_id	SWS_FT_FI5
Number of Residues	54
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:25621951

Chain	Residue	Details
A	LYS55
D	LYS55
D	LYS68
D	LYS104
E	LYS55
E	LYS68
E	LYS104
F	LYS55
F	LYS68
F	LYS104
G	LYS55
A	LYS68
G	LYS68
G	LYS104
H	LYS55
H	LYS68
H	LYS104
I	LYS55
I	LYS68
I	LYS104
J	LYS55
J	LYS68
A	LYS104
J	LYS104
K	LYS55
K	LYS68
K	LYS104
L	LYS55
L	LYS68
L	LYS104
M	LYS55
M	LYS68
M	LYS104
B	LYS55
N	LYS55
N	LYS68
N	LYS104
O	LYS55
O	LYS68
O	LYS104
P	LYS55
P	LYS68
P	LYS104
Q	LYS55
B	LYS68
Q	LYS68
Q	LYS104
R	LYS55
R	LYS68
R	LYS104
B	LYS104
C	LYS55
C	LYS68
C	LYS104

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