1VRS
Crystal structure of the disulfide-linked complex between the N-terminal and C-terminal domain of the electron transfer catalyst DsbD
Replaces: 1SE1Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0047134 | molecular_function | protein-disulfide reductase (NAD(P)) activity |
B | 0047134 | molecular_function | protein-disulfide reductase (NAD(P)) activity |
C | 0047134 | molecular_function | protein-disulfide reductase (NAD(P)) activity |
D | 0047134 | molecular_function | protein-disulfide reductase (NAD(P)) activity |
E | 0047134 | molecular_function | protein-disulfide reductase (NAD(P)) activity |
F | 0047134 | molecular_function | protein-disulfide reductase (NAD(P)) activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 378 |
Details | TOPO_DOM: Periplasmic => ECO:0000255 |
Chain | Residue | Details |
D | THR420-PRO546 | |
E | THR420-PRO546 | |
F | THR420-PRO546 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1l6p |
Chain | Residue | Details |
A | CYS109 | |
A | SER103 | |
A | TYR42 | |
A | ASP68 | |
A | TYR71 | |
A | PHE70 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1l6p |
Chain | Residue | Details |
B | CYS109 | |
B | SER103 | |
B | TYR42 | |
B | ASP68 | |
B | TYR71 | |
B | PHE70 |
site_id | CSA3 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1l6p |
Chain | Residue | Details |
C | CYS109 | |
C | SER103 | |
C | TYR42 | |
C | ASP68 | |
C | TYR71 | |
C | PHE70 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1l6p |
Chain | Residue | Details |
D | CYS461 | |
D | SER464 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1l6p |
Chain | Residue | Details |
E | CYS461 | |
E | SER464 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1l6p |
Chain | Residue | Details |
F | CYS461 | |
F | SER464 |
site_id | MCSA1 |
Number of Residues | |
Details | M-CSA 627 |
Chain | Residue | Details |
A | TYR42 | proton acceptor, proton donor, proton relay |
A | ASP68 | electrostatic stabiliser, proton acceptor, proton donor |
A | PHE70 | electrostatic stabiliser |
A | TYR71 | electrostatic stabiliser |
A | SER103 | electrofuge, hydride acceptor, nucleophile, proton donor |
A | CYS109 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
site_id | MCSA2 |
Number of Residues | |
Details | M-CSA 627 |
Chain | Residue | Details |
B | TYR42 | proton acceptor, proton donor, proton relay |
B | ASP68 | electrostatic stabiliser, proton acceptor, proton donor |
B | PHE70 | electrostatic stabiliser |
B | TYR71 | electrostatic stabiliser |
B | SER103 | electrofuge, hydride acceptor, nucleophile, proton donor |
B | CYS109 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
site_id | MCSA3 |
Number of Residues | |
Details | M-CSA 627 |
Chain | Residue | Details |
C | TYR42 | proton acceptor, proton donor, proton relay |
C | ASP68 | electrostatic stabiliser, proton acceptor, proton donor |
C | PHE70 | electrostatic stabiliser |
C | TYR71 | electrostatic stabiliser |
C | SER103 | electrofuge, hydride acceptor, nucleophile, proton donor |
C | CYS109 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |