Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003723 | molecular_function | RNA binding |
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 | 0005737 | cellular_component | cytoplasm |
A | 0005886 | cellular_component | plasma membrane |
A | 0006412 | biological_process | translation |
A | 0006414 | biological_process | translational elongation |
A | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
A | 0046677 | biological_process | response to antibiotic |
A | 0097216 | molecular_function | guanosine tetraphosphate binding |
B | 0003723 | molecular_function | RNA binding |
B | 0003746 | molecular_function | translation elongation factor activity |
B | 0003924 | molecular_function | GTPase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005525 | molecular_function | GTP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005886 | cellular_component | plasma membrane |
B | 0006412 | biological_process | translation |
B | 0006414 | biological_process | translational elongation |
B | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
B | 0046677 | biological_process | response to antibiotic |
B | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue MG A 401 |
Chain | Residue |
A | THR26 |
A | GDP403 |
A | HOH507 |
A | HOH513 |
A | HOH528 |
A | HOH535 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 402 |
Chain | Residue |
A | HOH530 |
B | GLU286 |
A | ASP355 |
A | HOH503 |
A | HOH520 |
site_id | AC3 |
Number of Residues | 18 |
Details | binding site for residue GDP A 403 |
Chain | Residue |
A | ASP22 |
A | HIS23 |
A | GLY24 |
A | LYS25 |
A | THR26 |
A | THR27 |
A | PHE47 |
A | ASN136 |
A | LYS137 |
A | ASP139 |
A | SER174 |
A | ALA175 |
A | LEU176 |
A | MG401 |
A | HOH507 |
A | HOH513 |
A | HOH525 |
A | HOH528 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue ACT A 404 |
Chain | Residue |
A | ARG124 |
A | GLY127 |
A | PRO129 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue ACT A 405 |
Chain | Residue |
A | MET113 |
A | PRO114 |
A | ARG117 |
A | ARG263 |
A | LYS264 |
A | LEU265 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue ACT A 406 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue EPE A 407 |
Chain | Residue |
A | LEU266 |
A | ASP267 |
A | GLU268 |
A | GLY269 |
A | ARG270 |
A | GLU273 |
A | HOH504 |
A | HOH531 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue BME A 408 |
Chain | Residue |
A | ARG289 |
B | LYS264 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue BME A 409 |
Chain | Residue |
A | ASP162 |
B | ASP110 |
B | PRO112 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MG B 401 |
Chain | Residue |
B | THR26 |
B | GDP403 |
B | HOH502 |
B | HOH503 |
B | HOH506 |
B | HOH539 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue MG B 402 |
Chain | Residue |
A | HOH518 |
A | HOH522 |
A | HOH524 |
A | HOH569 |
B | HOH519 |
B | HOH521 |
site_id | AD3 |
Number of Residues | 18 |
Details | binding site for residue GDP B 403 |
Chain | Residue |
B | ASP22 |
B | HIS23 |
B | GLY24 |
B | LYS25 |
B | THR26 |
B | THR27 |
B | PHE47 |
B | ASN136 |
B | LYS137 |
B | ASP139 |
B | MET140 |
B | SER174 |
B | ALA175 |
B | LEU176 |
B | MG401 |
B | HOH502 |
B | HOH503 |
B | HOH506 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue ACT B 404 |
Chain | Residue |
B | GLY84 |
B | HIS85 |
B | GLN115 |
site_id | AD5 |
Number of Residues | 5 |
Details | binding site for residue EPE B 405 |
Chain | Residue |
B | GLU268 |
B | ARG270 |
B | GLU273 |
B | HOH513 |
B | HOH523 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue CL B 406 |
Chain | Residue |
B | THR72 |
B | PRO73 |
B | THR74 |
B | ASP197 |
Functional Information from PROSITE/UniProt
site_id | PS00301 |
Number of Residues | 16 |
Details | G_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DNapeEKaRGITIntS |
Chain | Residue | Details |
A | ASP51-SER66 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY19 | |
A | ASP81 | |
A | ASN136 | |
B | GLY19 | |
B | ASP81 | |
B | ASN136 | |
Chain | Residue | Details |
A | SER2 | |
B | SER2 | |
Chain | Residue | Details |
A | LYS57 | |
B | LYS57 | |
Chain | Residue | Details |
A | LYS314 | |
B | LYS314 | |
Chain | Residue | Details |
A | GLU383 | |
B | GLU383 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 535 |
Chain | Residue | Details |
A | ASP22 | electrostatic stabiliser |
A | LYS25 | electrostatic stabiliser |
A | THR26 | metal ligand |
A | HIS85 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 535 |
Chain | Residue | Details |
B | ASP22 | electrostatic stabiliser |
B | LYS25 | electrostatic stabiliser |
B | THR26 | metal ligand |
B | HIS85 | electrostatic stabiliser |