1KK2
Structure of the large gamma subunit of initiation factor eIF2 from Pyrococcus abyssi-G235D mutant complexed with GDP-Mg2+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0001731 | biological_process | formation of translation preinitiation complex |
| A | 0003743 | molecular_function | translation initiation factor activity |
| A | 0003746 | molecular_function | translation elongation factor activity |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0006413 | biological_process | translational initiation |
| A | 0006414 | biological_process | translational elongation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 411 |
| Chain | Residue |
| A | CYS60 |
| A | CYS63 |
| A | CYS72 |
| A | CYS75 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 413 |
| Chain | Residue |
| A | HOH1093 |
| A | THR24 |
| A | GDP412 |
| A | HOH1086 |
| A | HOH1087 |
| A | HOH1090 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GDP A 412 |
| Chain | Residue |
| A | VAL19 |
| A | ASP20 |
| A | HIS21 |
| A | GLY22 |
| A | LYS23 |
| A | THR24 |
| A | THR25 |
| A | ASN145 |
| A | LYS146 |
| A | GLU148 |
| A | LEU149 |
| A | SER180 |
| A | ALA181 |
| A | LEU182 |
| A | MG413 |
| A | HOH1002 |
| A | HOH1084 |
| A | HOH1086 |
| A | HOH1087 |
| A | HOH1093 |
| A | HOH1159 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Region: {"description":"G1","evidences":[{"source":"UniProtKB","id":"Q980A5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Region: {"description":"G2","evidences":[{"source":"UniProtKB","id":"Q980A5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Region: {"description":"G3","evidences":[{"source":"UniProtKB","id":"Q980A5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Region: {"description":"G4","evidences":[{"source":"UniProtKB","id":"Q980A5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Region: {"description":"G5","evidences":[{"source":"UniProtKB","id":"Q980A5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11927566","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KK1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KK2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KK3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q980A5","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00119","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11927566","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KJZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KK0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KK1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KK2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KK3","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | ASP20 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ksj |
| Chain | Residue | Details |
| A | HIS93 |






