1D8T
CRYSTAL STRUCTURE OF ELONGATION FACTOR, TU (EF-TU-MGGDP) COMPLEXED WITH GE2270A, A THIAZOLYL PEPTIDE ANTIBIOTIC
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0016787 | molecular_function | hydrolase activity |
| A | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion 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 | 0016787 | molecular_function | hydrolase activity |
| B | 0032045 | cellular_component | guanyl-nucleotide exchange factor complex |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0097216 | molecular_function | guanosine tetraphosphate binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0031640 | biological_process | killing of cells of another organism |
| C | 0042742 | biological_process | defense response to bacterium |
| D | 0005576 | cellular_component | extracellular region |
| D | 0031640 | biological_process | killing of cells of another organism |
| D | 0042742 | biological_process | defense response to bacterium |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 998 |
| Chain | Residue |
| A | THR25 |
| A | GDP999 |
| A | HOH2018 |
| A | HOH2063 |
| A | HOH2064 |
| A | HOH2218 |
| site_id | AC2 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GDP A 999 |
| Chain | Residue |
| A | LYS24 |
| A | THR25 |
| A | THR26 |
| A | PHE46 |
| A | ASN135 |
| A | LYS136 |
| A | ASP138 |
| A | MET139 |
| A | SER173 |
| A | ALA174 |
| A | LEU175 |
| A | MG998 |
| A | HOH2017 |
| A | HOH2063 |
| A | HOH2064 |
| A | HOH2217 |
| A | HOH2218 |
| A | HOH2219 |
| A | ASP21 |
| A | HIS22 |
| A | GLY23 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 3002 |
| Chain | Residue |
| A | THR167 |
| A | PRO168 |
| A | ILE169 |
| A | HOH2115 |
| A | ACT3019 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 3003 |
| Chain | Residue |
| A | ARG123 |
| A | ASP370 |
| A | ALA389 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 3004 |
| Chain | Residue |
| A | ARG154 |
| A | ASP165 |
| A | SER221 |
| A | ACT3028 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 3005 |
| Chain | Residue |
| A | GLU152 |
| A | GLU155 |
| A | GLN159 |
| A | HOH2221 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 3006 |
| Chain | Residue |
| A | THR302 |
| A | LEU362 |
| A | ILE363 |
| A | HOH2172 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 3007 |
| Chain | Residue |
| A | VAL127 |
| A | ARG373 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 3010 |
| Chain | Residue |
| A | PRO113 |
| A | HOH2221 |
| A | HOH2222 |
| B | ACT3009 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 3013 |
| Chain | Residue |
| A | ARG171 |
| A | TRP184 |
| A | HOH2223 |
| A | ACT3023 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 3016 |
| Chain | Residue |
| A | ILE247 |
| A | GLU287 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 3017 |
| Chain | Residue |
| A | VAL391 |
| A | LEU392 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 3019 |
| Chain | Residue |
| A | ILE169 |
| A | VAL170 |
| A | ARG171 |
| A | LYS187 |
| A | GLU190 |
| A | ACT3002 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 3020 |
| Chain | Residue |
| A | GLU6 |
| A | GLY94 |
| A | ALA95 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 3021 |
| Chain | Residue |
| A | ASP50 |
| A | PRO82 |
| A | HOH2017 |
| site_id | BC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 3022 |
| Chain | Residue |
| A | SER65 |
| A | HIS66 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 3023 |
| Chain | Residue |
| A | VAL140 |
| A | ASP141 |
| A | ASP142 |
| A | GLU143 |
| A | LEU146 |
| A | ACT3013 |
| C | BB92 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 3025 |
| Chain | Residue |
| A | TYR129 |
| A | TYR198 |
| A | HOH2226 |
| A | HOH2227 |
| site_id | CC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT A 3026 |
| Chain | Residue |
| A | HIS84 |
| A | ASN355 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 3028 |
| Chain | Residue |
| A | ILE220 |
| A | SER221 |
| A | ACT3004 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 3030 |
| Chain | Residue |
| A | TYR39 |
| A | LEU189 |
| A | ALA192 |
| A | ASP196 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 998 |
| Chain | Residue |
| B | HOH2013 |
| B | HOH2140 |
| B | HOH2141 |
| B | THR25 |
| B | ASP50 |
| B | GDP999 |
| B | HOH2006 |
| site_id | CC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GDP B 999 |
| Chain | Residue |
| 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 | MG998 |
| B | HOH2004 |
| B | HOH2139 |
| B | HOH2140 |
| B | HOH2141 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 3001 |
| Chain | Residue |
| B | ARG154 |
| B | ILE169 |
| B | ACT3008 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 3008 |
| Chain | Residue |
| B | VAL170 |
| B | ARG171 |
| B | LYS187 |
| B | GLU190 |
| B | ACT3001 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 3009 |
| Chain | Residue |
| A | PRO111 |
| A | ACT3010 |
| B | ARG318 |
| B | HIS319 |
| B | THR320 |
| B | GLU378 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 3011 |
| Chain | Residue |
| A | PHE323 |
| A | GLU348 |
| B | VAL140 |
| B | ASP141 |
| B | ASP142 |
| site_id | DC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 3012 |
| Chain | Residue |
| B | GLU215 |
| B | ARG288 |
| B | TYR331 |
| B | ARG333 |
| B | HOH2087 |
| site_id | DC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 3014 |
| Chain | Residue |
| B | HIS84 |
| B | GLY353 |
| B | ASN355 |
| site_id | DC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 3015 |
| Chain | Residue |
| B | GLY41 |
| B | ALA42 |
| B | GLU68 |
| B | ASP70 |
| B | HOH2008 |
| site_id | DC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT B 3018 |
| Chain | Residue |
| B | ASP166 |
| site_id | DC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT B 3024 |
| Chain | Residue |
| B | GLU201 |
| B | HOH2144 |
| site_id | DC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT B 3027 |
| Chain | Residue |
| B | ASP336 |
| site_id | DC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 3029 |
| Chain | Residue |
| B | TYR39 |
| B | LEU189 |
| B | ASP196 |
| B | HOH2145 |
| B | HOH2146 |
| site_id | DC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NH2 C 15 |
| Chain | Residue |
| A | GLY222 |
| C | PRO14 |
| site_id | DC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NH2 D 15 |
| Chain | Residue |
| B | GLY222 |
| D | SER13 |
| D | PRO14 |
| site_id | EC1 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR CHAIN C OF THIOCILIN GE2270 |
| Chain | Residue |
| A | THR73 |
| A | GLU143 |
| A | ALA182 |
| A | GLU215 |
| A | ASP216 |
| A | GLY222 |
| A | ARG223 |
| A | VAL226 |
| A | THR228 |
| A | GLY229 |
| A | ARG230 |
| A | THR256 |
| A | GLY257 |
| A | VAL258 |
| A | GLU259 |
| A | PHE261 |
| A | ARG262 |
| A | ASN273 |
| A | VAL274 |
| A | GLY275 |
| A | LEU277 |
| A | HOH2024 |
| A | HOH2161 |
| A | ACT3023 |
| C | NH215 |
| C | HOH2002 |
| C | HOH2003 |
| site_id | EC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR CHAIN D OF THIOCILIN GE2270 |
| Chain | Residue |
| B | PRO72 |
| B | THR73 |
| B | GLU143 |
| B | GLU215 |
| B | ASP216 |
| B | PHE218 |
| B | ARG223 |
| B | VAL226 |
| B | THR228 |
| B | ARG230 |
| B | THR256 |
| B | GLY257 |
| B | VAL258 |
| B | GLU259 |
| B | PHE261 |
| B | ARG262 |
| B | LEU264 |
| B | ASN273 |
| B | VAL274 |
| B | GLY275 |
| B | LEU277 |
| B | HOH2097 |
| B | HOH2099 |
| D | NH215 |
| D | HOH2001 |
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 | 388 |
| Details | Domain: {"description":"tr-type G"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Region: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Region: {"description":"G2","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Region: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Region: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Region: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29546243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5OPD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"29546243","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5MI3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5OPD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"2022614","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"389663","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6997043","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7021545","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19150849","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24141193","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8416965","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 20434456 |
| Chain | Residue | Details |
| A | ASP21 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 20434456 |
| Chain | Residue | Details |
| B | ASP21 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 535 |
| Chain | Residue | Details |
| A | ASP21 | electrostatic stabiliser |
| A | LYS24 | electrostatic stabiliser |
| A | THR25 | metal ligand |
| A | HIS84 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 535 |
| Chain | Residue | Details |
| B | ASP21 | electrostatic stabiliser |
| B | LYS24 | electrostatic stabiliser |
| B | THR25 | metal ligand |
| B | HIS84 | electrostatic stabiliser |






