4X43

Structure of proline-free E. coli Thioredoxin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0015035	molecular_function	protein-disulfide reductase activity
A	0015036	molecular_function	disulfide oxidoreductase activity
A	0030337	molecular_function	DNA polymerase processivity factor activity
A	0045454	biological_process	cell redox homeostasis
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0015035	molecular_function	protein-disulfide reductase activity
B	0015036	molecular_function	disulfide oxidoreductase activity
B	0030337	molecular_function	DNA polymerase processivity factor activity
B	0045454	biological_process	cell redox homeostasis
C	0005515	molecular_function	protein binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0015035	molecular_function	protein-disulfide reductase activity
C	0015036	molecular_function	disulfide oxidoreductase activity
C	0030337	molecular_function	DNA polymerase processivity factor activity
C	0045454	biological_process	cell redox homeostasis

Functional Information from PROSITE/UniProt

site_id	PS00194
Number of Residues	19
Details	THIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGACKmIaaiL

Chain	Residue	Details
A	LEU24-LEU42

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	3
Details	SITE: Deprotonates C-terminal active site Cys

site_id	SWS_FT_FI3
Number of Residues	6
Details	SITE: Contributes to redox potential value

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18723842