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 | 20 |
Details | binding site for residue GNP A 401 |
Chain | Residue |
A | VAL20 |
A | ASP138 |
A | MET139 |
A | SER173 |
A | ALA174 |
A | LEU175 |
A | MG402 |
A | HOH511 |
A | HOH515 |
A | HOH517 |
A | HOH542 |
A | ASP21 |
A | HOH603 |
A | HIS22 |
A | GLY23 |
A | LYS24 |
A | THR25 |
A | THR26 |
A | ASN135 |
A | LYS136 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 402 |
Chain | Residue |
A | THR25 |
A | GNP401 |
A | HOH511 |
A | HOH515 |
A | HOH517 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL A 403 |
Chain | Residue |
A | ARG288 |
A | ARG377 |
A | HOH522 |
A | HOH577 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue GOL A 404 |
Chain | Residue |
A | ASP165 |
A | ASP166 |
A | THR167 |
A | HOH557 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue GOL A 405 |
Chain | Residue |
A | GLU183 |
A | TRP184 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 406 |
Chain | Residue |
A | LEU120 |
A | GLU307 |
A | ASN355 |
A | HOH520 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 407 |
Chain | Residue |
A | MET260 |
A | PHE261 |
A | ARG262 |
A | LYS263 |
B | ARG288 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue PEG A 408 |
Chain | Residue |
A | LEU211 |
A | ARG233 |
A | ARG333 |
A | ASP369 |
A | LEU372 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue PEG A 409 |
Chain | Residue |
A | PRO111 |
A | MET112 |
A | PRO113 |
A | ARG116 |
A | HOH531 |
site_id | AD1 |
Number of Residues | 3 |
Details | binding site for residue PEG A 410 |
Chain | Residue |
A | HIS84 |
A | ALA85 |
A | GLN114 |
site_id | AD2 |
Number of Residues | 21 |
Details | binding site for residue GNP B 401 |
Chain | Residue |
B | VAL20 |
B | ASP21 |
B | HIS22 |
B | GLY23 |
B | LYS24 |
B | THR25 |
B | THR26 |
B | PHE46 |
B | ASN135 |
B | LYS136 |
B | ASP138 |
B | MET139 |
B | SER173 |
B | ALA174 |
B | LEU175 |
B | MG402 |
B | HOH510 |
B | HOH528 |
B | HOH555 |
B | HOH574 |
B | HOH585 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue MG B 402 |
Chain | Residue |
B | THR25 |
B | GNP401 |
B | HOH510 |
B | HOH528 |
B | HOH555 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | ARG318 |
B | TYR326 |
B | HOH503 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
B | TYR331 |
B | ARG333 |
B | ARG373 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue GOL B 405 |
Chain | Residue |
B | ARG327 |
B | THR338 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue GOL B 406 |
Chain | Residue |
A | ARG283 |
B | ARG262 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 407 |
Chain | Residue |
A | ARG288 |
B | MET260 |
B | PHE261 |
B | ARG262 |
B | LYS263 |
B | HOH543 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 408 |
Chain | Residue |
B | PRO111 |
B | MET112 |
B | PRO113 |
B | ARG116 |
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 | ASP50-SER65 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY18 | |
A | ASP80 | |
A | ASN135 | |
B | GLY18 | |
B | ASP80 | |
B | ASN135 | |
Chain | Residue | Details |
A | SER1 | |
B | SER1 | |
Chain | Residue | Details |
A | LYS37 | |
B | LYS294 | |
A | LYS176 | |
A | LYS248 | |
A | LYS252 | |
A | LYS294 | |
B | LYS37 | |
B | LYS176 | |
B | LYS248 | |
B | LYS252 | |
Chain | Residue | Details |
A | LYS56 | |
B | LYS56 | |
Chain | Residue | Details |
A | LYS313 | |
B | LYS313 | |
Chain | Residue | Details |
A | THR382 | |
B | THR382 | |