2FCH
Crystal Structure of Thioredoxin Mutant G74S
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 |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0015035 | molecular_function | protein-disulfide reductase activity |
D | 0015036 | molecular_function | disulfide oxidoreductase activity |
D | 0030337 | molecular_function | DNA polymerase processivity factor activity |
D | 0045454 | biological_process | cell redox homeostasis |
E | 0005515 | molecular_function | protein binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0015035 | molecular_function | protein-disulfide reductase activity |
E | 0015036 | molecular_function | disulfide oxidoreductase activity |
E | 0030337 | molecular_function | DNA polymerase processivity factor activity |
E | 0045454 | biological_process | cell redox homeostasis |
F | 0005515 | molecular_function | protein binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0015035 | molecular_function | protein-disulfide reductase activity |
F | 0015036 | molecular_function | disulfide oxidoreductase activity |
F | 0030337 | molecular_function | DNA polymerase processivity factor activity |
F | 0045454 | biological_process | cell redox homeostasis |
G | 0005515 | molecular_function | protein binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0005829 | cellular_component | cytosol |
G | 0015035 | molecular_function | protein-disulfide reductase activity |
G | 0015036 | molecular_function | disulfide oxidoreductase activity |
G | 0030337 | molecular_function | DNA polymerase processivity factor activity |
G | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD D 501 |
Chain | Residue |
B | TYR70 |
D | TYR70 |
D | GLY71 |
D | THR89 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD E 502 |
Chain | Residue |
E | ILE60 |
E | ALA67 |
E | ARG73 |
E | SER74 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD E 503 |
Chain | Residue |
A | THR89 |
E | TYR70 |
E | GLY71 |
E | THR89 |
A | TYR70 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MPD G 504 |
Chain | Residue |
F | TRP31 |
F | ILE60 |
F | ILE72 |
F | ARG73 |
F | SER74 |
G | TYR70 |
G | GLY71 |
G | HOH508 |
site_id | AC5 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE MPD D 505 |
Chain | Residue |
B | ARG73 |
B | HOH114 |
B | HOH115 |
C | ILE41 |
C | GLU44 |
C | LYS96 |
C | HOH120 |
D | TYR70 |
D | GLY84 |
D | GLU85 |
D | VAL86 |
D | HOH507 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD D 506 |
Chain | Residue |
D | ILE60 |
D | ILE72 |
D | ARG73 |
E | LYS36 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MPD A 507 |
Chain | Residue |
A | ILE72 |
A | HOH509 |
B | LYS36 |
B | PRO40 |
Functional Information from PROSITE/UniProt
site_id | PS00194 |
Number of Residues | 19 |
Details | THIOREDOXIN_1 Thioredoxin family active site. LVdFWaeWCGPCKmIapiL |
Chain | Residue | Details |
A | LEU24-LEU42 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | GLY33 | |
E | LYS36 | |
F | GLY33 | |
F | LYS36 | |
G | GLY33 | |
G | LYS36 | |
A | LYS36 | |
B | GLY33 | |
B | LYS36 | |
C | GLY33 | |
C | LYS36 | |
D | GLY33 | |
D | LYS36 | |
E | GLY33 |
site_id | SWS_FT_FI2 |
Number of Residues | 7 |
Details | SITE: Deprotonates C-terminal active site Cys |
Chain | Residue | Details |
A | PHE27 | |
B | PHE27 | |
C | PHE27 | |
D | PHE27 | |
E | PHE27 | |
F | PHE27 | |
G | PHE27 |
site_id | SWS_FT_FI3 |
Number of Residues | 14 |
Details | SITE: Contributes to redox potential value |
Chain | Residue | Details |
A | PRO34 | |
E | CYS35 | |
F | PRO34 | |
F | CYS35 | |
G | PRO34 | |
G | CYS35 | |
A | CYS35 | |
B | PRO34 | |
B | CYS35 | |
C | PRO34 | |
C | CYS35 | |
D | PRO34 | |
D | CYS35 | |
E | PRO34 |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
A | TYR70 | |
B | TYR70 | |
C | TYR70 | |
D | TYR70 | |
E | TYR70 | |
F | TYR70 | |
G | TYR70 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
A | PRO34 | |
A | CYS35 | |
A | CYS32 | |
A | GLY33 |
site_id | CSA10 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
C | CYS35 | |
C | CYS32 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
D | CYS35 | |
D | CYS32 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
E | CYS35 | |
E | CYS32 |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
F | CYS35 | |
F | CYS32 |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
G | CYS35 | |
G | CYS32 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
B | PRO34 | |
B | CYS35 | |
B | CYS32 | |
B | GLY33 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
C | PRO34 | |
C | CYS35 | |
C | CYS32 | |
C | GLY33 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
D | PRO34 | |
D | CYS35 | |
D | CYS32 | |
D | GLY33 |
site_id | CSA5 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
E | PRO34 | |
E | CYS35 | |
E | CYS32 | |
E | GLY33 |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
F | PRO34 | |
F | CYS35 | |
F | CYS32 | |
F | GLY33 |
site_id | CSA7 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
G | PRO34 | |
G | CYS35 | |
G | CYS32 | |
G | GLY33 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
A | CYS35 | |
A | CYS32 |
site_id | CSA9 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1mek |
Chain | Residue | Details |
B | CYS35 | |
B | CYS32 |