4EKZ
Crystal structure of reduced hPDI (abb'xa')
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003756 | molecular_function | protein disulfide isomerase activity |
| A | 0003779 | molecular_function | actin binding |
| A | 0004656 | molecular_function | procollagen-proline 4-dioxygenase activity |
| A | 0005178 | molecular_function | integrin binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005793 | cellular_component | endoplasmic reticulum-Golgi intermediate compartment |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0006457 | biological_process | protein folding |
| A | 0009897 | cellular_component | external side of plasma membrane |
| A | 0015035 | molecular_function | protein-disulfide reductase activity |
| A | 0016222 | cellular_component | procollagen-proline 4-dioxygenase complex |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016972 | molecular_function | thiol oxidase activity |
| A | 0018401 | biological_process | peptidyl-proline hydroxylation to 4-hydroxy-L-proline |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0030027 | cellular_component | lamellipodium |
| A | 0030070 | biological_process | insulin processing |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0034663 | cellular_component | endoplasmic reticulum chaperone complex |
| A | 0034975 | biological_process | protein folding in endoplasmic reticulum |
| A | 0034976 | biological_process | response to endoplasmic reticulum stress |
| A | 0035722 | biological_process | interleukin-12-mediated signaling pathway |
| A | 0038155 | biological_process | interleukin-23-mediated signaling pathway |
| A | 0042470 | cellular_component | melanosome |
| A | 0044877 | molecular_function | protein-containing complex binding |
| A | 0045785 | biological_process | positive regulation of cell adhesion |
| A | 0046598 | biological_process | positive regulation of viral entry into host cell |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071456 | biological_process | cellular response to hypoxia |
| A | 1900026 | biological_process | positive regulation of substrate adhesion-dependent cell spreading |
| A | 1902175 | biological_process | regulation of oxidative stress-induced intrinsic apoptotic signaling pathway |
| A | 2000406 | biological_process | positive regulation of T cell migration |
Functional Information from PROSITE/UniProt
| site_id | PS00194 |
| Number of Residues | 19 |
| Details | THIOREDOXIN_1 Thioredoxin family active site. LVeFYapWCGHCKaLapeY |
| Chain | Residue | Details |
| A | LEU45-TYR63 | |
| A | PHE389-TRP407 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 116 |
| Details | Domain: {"description":"Thioredoxin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 126 |
| Details | Domain: {"description":"Thioredoxin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Contributes to redox potential value"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Lowers pKa of C-terminal Cys of first active site"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Contributes to redox potential value","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Lowers pKa of C-terminal Cys of second active site","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P09103","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P09103","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"32149426","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32149426","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 191 |
| Chain | Residue | Details |
| A | CYS53 | nucleofuge, nucleophile, proton acceptor, proton donor |
| A | GLY54 | activator, modifies pKa |
| A | HIS55 | modifies pKa, proton acceptor, proton donor |
| A | CYS56 |
