8PHD
Structure of Human Cdc123 bound to domain 3 of eIF2 gamma and ATP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006457 | biological_process | protein folding |
A | 0044183 | molecular_function | protein folding chaperone |
A | 0046872 | molecular_function | metal ion binding |
A | 1905143 | biological_process | eukaryotic translation initiation factor 2 complex assembly |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0005515 | molecular_function | protein binding |
C | 0005524 | molecular_function | ATP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006457 | biological_process | protein folding |
C | 0044183 | molecular_function | protein folding chaperone |
C | 0046872 | molecular_function | metal ion binding |
C | 1905143 | biological_process | eukaryotic translation initiation factor 2 complex assembly |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:37507029, ECO:0007744|PDB:8PHD, ECO:0007744|PDB:8PHV |
Chain | Residue | Details |
C | LYS168 | |
C | CYS170 | |
C | GLU177 | |
C | ARG179 | |
C | ARG193 | |
A | LYS168 | |
A | CYS170 | |
A | GLU177 | |
A | ARG179 | |
A | ARG193 | |
C | LYS104 | |
C | ALA109 | |
A | LYS104 | |
A | ALA109 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:37507029, ECO:0007744|PDB:8PHV |
Chain | Residue | Details |
A | TRP107 | |
C | TRP107 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9P7N5 |
Chain | Residue | Details |
A | ARG111 | |
A | ARG167 | |
A | TRP169 | |
A | ASP233 | |
C | ARG111 | |
C | ARG167 | |
C | TRP169 | |
C | ASP233 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:37507029, ECO:0007744|PDB:8PHD |
Chain | Residue | Details |
A | ASP246 | |
A | ASN248 | |
C | ASP246 | |
C | ASN248 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | SER60 | |
C | SER60 |