Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6B4C

Structure of Viperin from Trichoderma virens

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0005739	cellular_component	mitochondrion
A	0005783	cellular_component	endoplasmic reticulum
A	0046872	molecular_function	metal ion binding
A	0050778	biological_process	positive regulation of immune response
A	0051536	molecular_function	iron-sulfur cluster binding
A	0051539	molecular_function	4 iron, 4 sulfur cluster binding
A	0051607	biological_process	defense response to virus
B	0003824	molecular_function	catalytic activity
B	0005739	cellular_component	mitochondrion
B	0005783	cellular_component	endoplasmic reticulum
B	0046872	molecular_function	metal ion binding
B	0050778	biological_process	positive regulation of immune response
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0051607	biological_process	defense response to virus
C	0003824	molecular_function	catalytic activity
C	0005739	cellular_component	mitochondrion
C	0005783	cellular_component	endoplasmic reticulum
C	0046872	molecular_function	metal ion binding
C	0050778	biological_process	positive regulation of immune response
C	0051536	molecular_function	iron-sulfur cluster binding
C	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0051607	biological_process	defense response to virus
D	0003824	molecular_function	catalytic activity
D	0005739	cellular_component	mitochondrion
D	0005783	cellular_component	endoplasmic reticulum
D	0046872	molecular_function	metal ion binding
D	0050778	biological_process	positive regulation of immune response
D	0051536	molecular_function	iron-sulfur cluster binding
D	0051539	molecular_function	4 iron, 4 sulfur cluster binding
D	0051607	biological_process	defense response to virus
E	0003824	molecular_function	catalytic activity
E	0005739	cellular_component	mitochondrion
E	0005783	cellular_component	endoplasmic reticulum
E	0046872	molecular_function	metal ion binding
E	0050778	biological_process	positive regulation of immune response
E	0051536	molecular_function	iron-sulfur cluster binding
E	0051539	molecular_function	4 iron, 4 sulfur cluster binding
E	0051607	biological_process	defense response to virus
F	0003824	molecular_function	catalytic activity
F	0005739	cellular_component	mitochondrion
F	0005783	cellular_component	endoplasmic reticulum
F	0046872	molecular_function	metal ion binding
F	0050778	biological_process	positive regulation of immune response
F	0051536	molecular_function	iron-sulfur cluster binding
F	0051539	molecular_function	4 iron, 4 sulfur cluster binding
F	0051607	biological_process	defense response to virus
G	0003824	molecular_function	catalytic activity
G	0005739	cellular_component	mitochondrion
G	0005783	cellular_component	endoplasmic reticulum
G	0046872	molecular_function	metal ion binding
G	0050778	biological_process	positive regulation of immune response
G	0051536	molecular_function	iron-sulfur cluster binding
G	0051539	molecular_function	4 iron, 4 sulfur cluster binding
G	0051607	biological_process	defense response to virus
H	0003824	molecular_function	catalytic activity
H	0005739	cellular_component	mitochondrion
H	0005783	cellular_component	endoplasmic reticulum
H	0046872	molecular_function	metal ion binding
H	0050778	biological_process	positive regulation of immune response
H	0051536	molecular_function	iron-sulfur cluster binding
H	0051539	molecular_function	4 iron, 4 sulfur cluster binding
H	0051607	biological_process	defense response to virus
I	0003824	molecular_function	catalytic activity
I	0005739	cellular_component	mitochondrion
I	0005783	cellular_component	endoplasmic reticulum
I	0046872	molecular_function	metal ion binding
I	0050778	biological_process	positive regulation of immune response
I	0051536	molecular_function	iron-sulfur cluster binding
I	0051539	molecular_function	4 iron, 4 sulfur cluster binding
I	0051607	biological_process	defense response to virus
J	0003824	molecular_function	catalytic activity
J	0005739	cellular_component	mitochondrion
J	0005783	cellular_component	endoplasmic reticulum
J	0046872	molecular_function	metal ion binding
J	0050778	biological_process	positive regulation of immune response
J	0051536	molecular_function	iron-sulfur cluster binding
J	0051539	molecular_function	4 iron, 4 sulfur cluster binding
J	0051607	biological_process	defense response to virus
K	0003824	molecular_function	catalytic activity
K	0005739	cellular_component	mitochondrion
K	0005783	cellular_component	endoplasmic reticulum
K	0046872	molecular_function	metal ion binding
K	0050778	biological_process	positive regulation of immune response
K	0051536	molecular_function	iron-sulfur cluster binding
K	0051539	molecular_function	4 iron, 4 sulfur cluster binding
K	0051607	biological_process	defense response to virus
L	0003824	molecular_function	catalytic activity
L	0005739	cellular_component	mitochondrion
L	0005783	cellular_component	endoplasmic reticulum
L	0046872	molecular_function	metal ion binding
L	0050778	biological_process	positive regulation of immune response
L	0051536	molecular_function	iron-sulfur cluster binding
L	0051539	molecular_function	4 iron, 4 sulfur cluster binding
L	0051607	biological_process	defense response to virus

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue SO4 A 401

Chain	Residue
A	LYS163
A	ARG188
A	LYS190

site_id	AC2
Number of Residues	2
Details	binding site for residue SO4 A 402

Chain	Residue
A	ARG226
A	HOH507

site_id	AC3
Number of Residues	8
Details	binding site for residue FLC A 403

Chain	Residue
A	HOH505
G	THR133
G	LYS136
G	HOH505
A	TYR78
A	PRO79
A	LYS80
A	PHE81

site_id	AC4
Number of Residues	2
Details	binding site for residue SO4 B 401

Chain	Residue
B	LYS163
B	LYS190

site_id	AC5
Number of Residues	1
Details	binding site for residue SO4 B 402

Chain	Residue
B	ARG226

site_id	AC6
Number of Residues	8
Details	binding site for residue FLC B 403

Chain	Residue
B	TYR78
B	PRO79
B	LYS80
B	PHE81
B	HOH514
B	HOH539
J	THR133
J	LYS136

site_id	AC7
Number of Residues	3
Details	binding site for residue SO4 C 401

Chain	Residue
C	LYS163
C	ARG188
C	LYS190

site_id	AC8
Number of Residues	3
Details	binding site for residue SO4 C 402

Chain	Residue
C	ARG222
C	ARG226
C	HOH502

site_id	AC9
Number of Residues	7
Details	binding site for residue FLC C 403

Chain	Residue
C	TYR78
C	PRO79
C	LYS80
C	PHE81
D	THR133
D	LYS136
D	PHE171

site_id	AD1
Number of Residues	3
Details	binding site for residue SO4 D 401

Chain	Residue
D	LYS163
D	ARG188
D	LYS190

site_id	AD2
Number of Residues	2
Details	binding site for residue SO4 D 402

Chain	Residue
D	ARG226
D	HOH513

site_id	AD3
Number of Residues	7
Details	binding site for residue FLC D 403

Chain	Residue
D	TYR78
D	PRO79
D	LYS80
D	PHE81
K	THR133
K	LYS136
K	HOH502

site_id	AD4
Number of Residues	3
Details	binding site for residue SO4 E 401

Chain	Residue
E	LYS163
E	ARG188
E	LYS190

site_id	AD5
Number of Residues	2
Details	binding site for residue SO4 E 402

Chain	Residue
E	ARG222
E	ARG226

site_id	AD6
Number of Residues	7
Details	binding site for residue FLC E 403

Chain	Residue
E	TYR78
E	PRO79
E	LYS80
E	PHE81
E	HOH508
H	THR133
H	LYS136

site_id	AD7
Number of Residues	3
Details	binding site for residue SO4 F 401

Chain	Residue
F	LYS163
F	ARG188
F	LYS190

site_id	AD8
Number of Residues	1
Details	binding site for residue SO4 F 402

Chain	Residue
F	ARG226

site_id	AD9
Number of Residues	8
Details	binding site for residue FLC F 403

Chain	Residue
A	THR133
A	LYS136
F	TYR78
F	PRO79
F	LYS80
F	PHE81
F	HOH507
F	HOH526

site_id	AE1
Number of Residues	4
Details	binding site for residue SO4 G 402

Chain	Residue
G	ARG222
G	ARG226
G	HOH502
G	HOH532

site_id	AE2
Number of Residues	8
Details	binding site for residue FLC G 403

Chain	Residue
F	THR133
F	LYS136
F	HOH502
G	TYR78
G	PRO79
G	LYS80
G	PHE81
G	HOH508

site_id	AE3
Number of Residues	3
Details	binding site for residue SO4 H 401

Chain	Residue
H	LYS163
H	ARG188
H	LYS190

site_id	AE4
Number of Residues	1
Details	binding site for residue SO4 H 402

Chain	Residue
H	ARG226

site_id	AE5
Number of Residues	8
Details	binding site for residue FLC H 403

Chain	Residue
H	TYR78
H	PRO79
H	LYS80
H	PHE81
H	HOH507
L	THR133
L	LYS136
L	PHE171

site_id	AE6
Number of Residues	3
Details	binding site for residue SO4 I 401

Chain	Residue
I	LYS190
I	LYS163
I	ARG188

site_id	AE7
Number of Residues	1
Details	binding site for residue SO4 I 402

Chain	Residue
I	ARG226

site_id	AE8
Number of Residues	7
Details	binding site for residue FLC I 403

Chain	Residue
B	THR133
B	LYS136
B	HOH507
I	TYR78
I	PRO79
I	LYS80
I	PHE81

site_id	AE9
Number of Residues	3
Details	binding site for residue SO4 J 401

Chain	Residue
J	LYS163
J	ARG188
J	LYS190

site_id	AF1
Number of Residues	3
Details	binding site for residue SO4 J 402

Chain	Residue
J	ARG222
J	ARG226
J	HOH512

site_id	AF2
Number of Residues	7
Details	binding site for residue FLC J 403

Chain	Residue
I	THR133
I	LYS136
J	TYR78
J	PRO79
J	LYS80
J	PHE81
J	HOH506

site_id	AF3
Number of Residues	3
Details	binding site for residue SO4 K 401

Chain	Residue
K	LYS163
K	ARG188
K	LYS190

site_id	AF4
Number of Residues	2
Details	binding site for residue SO4 K 402

Chain	Residue
K	ARG226
K	HOH505

site_id	AF5
Number of Residues	3
Details	binding site for residue SO4 L 401

Chain	Residue
L	LYS163
L	ARG188
L	LYS190

site_id	AF6
Number of Residues	1
Details	binding site for residue SO4 L 402

Chain	Residue
L	ARG226

site_id	AF7
Number of Residues	6
Details	binding site for residue FLC L 403

Chain	Residue
E	THR133
E	LYS136
L	TYR78
L	PRO79
L	LYS80
L	PHE81

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