3PEN
Structure of archaeal initiation factor aIF2gamma subunit delta 37-47 from Sulfolobus solfataricus in the GDP-bound form.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000049 | molecular_function | tRNA 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 | 0005515 | molecular_function | protein binding |
A | 0005525 | molecular_function | GTP binding |
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 | 22 |
Details | BINDING SITE FOR RESIDUE GDP A 416 |
Chain | Residue |
A | ASP19 |
A | ASP152 |
A | SER184 |
A | ALA185 |
A | LEU186 |
A | MG419 |
A | HOH530 |
A | HOH574 |
A | HOH580 |
A | HOH622 |
A | HOH626 |
A | HIS20 |
A | HOH638 |
A | HOH652 |
A | HOH660 |
A | GLY21 |
A | LYS22 |
A | THR23 |
A | THR24 |
A | HOH41 |
A | ASN149 |
A | LYS150 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 5GP A 1 |
Chain | Residue |
A | PHE221 |
A | VAL223 |
A | LYS234 |
A | SER278 |
A | ARG280 |
A | GLY282 |
A | ALA296 |
A | GLY298 |
A | HOH661 |
A | HOH668 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 417 |
Chain | Residue |
A | THR54 |
A | THR70 |
A | HOH591 |
A | HOH594 |
A | HOH603 |
A | HOH611 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 418 |
Chain | Residue |
A | VAL151 |
A | VAL154 |
A | TRP327 |
A | ASN328 |
A | HOH582 |
A | HOH596 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 419 |
Chain | Residue |
A | THR23 |
A | LYS48 |
A | GDP416 |
A | HOH574 |
A | HOH589 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 420 |
Chain | Residue |
A | GLU66 |
A | TYR68 |
A | ASP192 |
A | HOH581 |
A | HOH617 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 421 |
Chain | Residue |
A | MET111 |
A | HOH588 |
A | HOH601 |
A | HOH610 |
A | HOH615 |
A | HOH616 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00119, ECO:0000269|PubMed:25690901, ECO:0007744|PDB:4RD1 |
Chain | Residue | Details |
A | ASP19 | |
A | ASN55 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00119, ECO:0000269|PubMed:16407071, ECO:0000269|PubMed:25690901, ECO:0007744|PDB:2AHO |
Chain | Residue | Details |
A | THR23 | |
A | GLY57 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q8U082, ECO:0000255|HAMAP-Rule:MF_00119 |
Chain | Residue | Details |
A | THR70 | |
A | SER73 | |
A | PHE85 | |
A | ARG88 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00119, ECO:0000269|PubMed:25690901, ECO:0007744|PDB:4RCY, ECO:0007744|PDB:4RD1 |
Chain | Residue | Details |
A | LEU160 | |
A | ILE195 |