4ACB
CRYSTAL STRUCTURE OF TRANSLATION ELONGATION FACTOR SELB FROM METHANOCOCCUS MARIPALUDIS IN COMPLEX WITH THE GTP ANALOGUE GPPNHP
Replaces: 1WB3Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0001514 | biological_process | selenocysteine incorporation |
A | 0003723 | molecular_function | RNA binding |
A | 0003746 | molecular_function | translation elongation factor activity |
A | 0003924 | molecular_function | GTPase activity |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006412 | biological_process | translation |
A | 0006414 | biological_process | translational elongation |
A | 0046872 | molecular_function | metal ion binding |
B | 0001514 | biological_process | selenocysteine incorporation |
B | 0003723 | molecular_function | RNA binding |
B | 0003746 | molecular_function | translation elongation factor activity |
B | 0003924 | molecular_function | GTPase activity |
B | 0005525 | molecular_function | GTP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006412 | biological_process | translation |
B | 0006414 | biological_process | translational elongation |
B | 0046872 | molecular_function | metal ion binding |
C | 0001514 | biological_process | selenocysteine incorporation |
C | 0003723 | molecular_function | RNA binding |
C | 0003746 | molecular_function | translation elongation factor activity |
C | 0003924 | molecular_function | GTPase activity |
C | 0005525 | molecular_function | GTP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0006412 | biological_process | translation |
C | 0006414 | biological_process | translational elongation |
C | 0046872 | molecular_function | metal ion binding |
D | 0001514 | biological_process | selenocysteine incorporation |
D | 0003723 | molecular_function | RNA binding |
D | 0003746 | molecular_function | translation elongation factor activity |
D | 0003924 | molecular_function | GTPase activity |
D | 0005525 | molecular_function | GTP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0006412 | biological_process | translation |
D | 0006414 | biological_process | translational elongation |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE GNP A 1469 |
Chain | Residue |
A | ILE14 |
A | ASP122 |
A | SER155 |
A | ALA156 |
A | LYS157 |
A | MG1470 |
A | HOH2001 |
A | HOH2002 |
A | ASP15 |
A | GLY17 |
A | LYS18 |
A | THR19 |
A | THR20 |
A | THR46 |
A | GLY68 |
A | LYS120 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1470 |
Chain | Residue |
A | THR19 |
A | THR46 |
A | GNP1469 |
A | HOH2001 |
A | HOH2002 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE GDP B 1469 |
Chain | Residue |
B | HIS13 |
B | ILE14 |
B | ASP15 |
B | HIS16 |
B | GLY17 |
B | LYS18 |
B | THR19 |
B | THR20 |
B | LYS120 |
B | ASP122 |
B | ASN123 |
B | ALA156 |
B | LYS157 |
B | MG1470 |
B | HOH2001 |
B | HOH2002 |
B | HOH2004 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 1470 |
Chain | Residue |
B | THR19 |
B | GDP1469 |
B | HOH2001 |
B | HOH2002 |
B | HOH2003 |
B | HOH2004 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 1471 |
Chain | Residue |
B | ARG74 |
B | ARG262 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 1472 |
Chain | Residue |
B | LYS197 |
B | GLY198 |
C | LYS55 |
site_id | AC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE DXC B 1473 |
Chain | Residue |
B | ILE47 |
B | ASP48 |
B | ILE49 |
B | GLY50 |
B | PHE51 |
B | VAL202 |
B | GLN233 |
C | ARG-2 |
C | PRO195 |
site_id | AC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 5GP B 1474 |
Chain | Residue |
A | ARG230 |
A | SER238 |
B | PRO96 |
B | LYS97 |
B | THR98 |
B | MET104 |
B | LEU105 |
B | ILE139 |
B | THR143 |
B | ILE288 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 C 1471 |
Chain | Residue |
C | ASP108 |
C | HIS109 |
C | LYS284 |
C | ILE285 |
C | SER286 |
C | ASP287 |
C | SO41472 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 C 1472 |
Chain | Residue |
C | HIS144 |
C | LYS147 |
C | ASP287 |
C | SO41471 |
site_id | BC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 1473 |
Chain | Residue |
C | ARG465 |
C | ARG466 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DXC C 1475 |
Chain | Residue |
B | PRO195 |
C | ILE47 |
C | ASP48 |
C | ILE49 |
C | GLY50 |
C | PHE51 |
C | VAL202 |
C | GLN233 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DXC C 1476 |
Chain | Residue |
C | ARG-2 |
C | PRO-1 |
C | HIS0 |
C | MET1 |
C | ILE196 |
C | ALA199 |
C | ARG230 |
C | SER231 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DXC C 1477 |
Chain | Residue |
C | ILE139 |
C | LYS290 |
C | THR366 |
C | LEU368 |
C | DXC1480 |
C | PRO96 |
C | ARG131 |
site_id | BC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE DXC C 1478 |
Chain | Residue |
C | SER121 |
C | ASP122 |
C | ALA124 |
C | THR158 |
C | PHE160 |
C | LEU392 |
C | ARG393 |
C | GLU394 |
C | GLU427 |
C | ILE460 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DXC C 1479 |
Chain | Residue |
C | THR126 |
C | ILE129 |
C | GLU133 |
C | LEU392 |
C | SER425 |
C | ASN462 |
site_id | BC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE DXC C 1480 |
Chain | Residue |
C | ARG131 |
C | ILE135 |
C | SER138 |
C | LYS290 |
C | LYS290 |
C | GLU331 |
C | ILE333 |
C | SER334 |
C | DXC1477 |