2A1A
PKR kinase domain-eIF2alpha Complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003676 | molecular_function | nucleic acid binding |
A | 0003723 | molecular_function | RNA binding |
A | 0003743 | molecular_function | translation initiation factor activity |
B | 0004672 | molecular_function | protein kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGFGQVFkAkhridgkt..........YVIK |
Chain | Residue | Details |
B | ILE273-LYS296 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
Chain | Residue | Details |
B | GLN427 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
Chain | Residue | Details |
B | ILE273 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
B | LYS296 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:16179258, ECO:0000305|PubMed:31246429 |
Chain | Residue | Details |
B | ARG445 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000305|PubMed:11152499 |
Chain | Residue | Details |
B | THR258 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16373505 |
Chain | Residue | Details |
B | TYR293 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:11337501, ECO:0000269|PubMed:16179258 |
Chain | Residue | Details |
B | GLN459 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:11337501, ECO:0000269|PubMed:20685959 |
Chain | Residue | Details |
B | ASP464 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
B | VAL469 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |