5C8Y
Crystal structure of T2R-TTL-Plinabulin complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000226 | biological_process | microtubule cytoskeleton organization |
A | 0000278 | biological_process | mitotic cell cycle |
A | 0005200 | molecular_function | structural constituent of cytoskeleton |
A | 0005525 | molecular_function | GTP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005856 | cellular_component | cytoskeleton |
A | 0005874 | cellular_component | microtubule |
A | 0007017 | biological_process | microtubule-based process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000226 | biological_process | microtubule cytoskeleton organization |
B | 0000278 | biological_process | mitotic cell cycle |
B | 0003924 | molecular_function | GTPase activity |
B | 0005200 | molecular_function | structural constituent of cytoskeleton |
B | 0005525 | molecular_function | GTP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005856 | cellular_component | cytoskeleton |
B | 0005874 | cellular_component | microtubule |
B | 0007017 | biological_process | microtubule-based process |
B | 0046872 | molecular_function | metal ion binding |
C | 0000226 | biological_process | microtubule cytoskeleton organization |
C | 0000278 | biological_process | mitotic cell cycle |
C | 0005200 | molecular_function | structural constituent of cytoskeleton |
C | 0005525 | molecular_function | GTP binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005856 | cellular_component | cytoskeleton |
C | 0005874 | cellular_component | microtubule |
C | 0007017 | biological_process | microtubule-based process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0000226 | biological_process | microtubule cytoskeleton organization |
D | 0000278 | biological_process | mitotic cell cycle |
D | 0003924 | molecular_function | GTPase activity |
D | 0005200 | molecular_function | structural constituent of cytoskeleton |
D | 0005525 | molecular_function | GTP binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005856 | cellular_component | cytoskeleton |
D | 0005874 | cellular_component | microtubule |
D | 0007017 | biological_process | microtubule-based process |
D | 0046872 | molecular_function | metal ion binding |
E | 0031110 | biological_process | regulation of microtubule polymerization or depolymerization |
F | 0036211 | biological_process | protein modification process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | binding site for residue GTP A 501 |
Chain | Residue |
A | GLY10 |
A | GLY143 |
A | GLY144 |
A | THR145 |
A | GLY146 |
A | SER178 |
A | GLU183 |
A | ASN206 |
A | TYR224 |
A | ASN228 |
A | ILE231 |
A | GLN11 |
A | MG502 |
A | HOH618 |
A | HOH629 |
B | LYS252 |
B | HOH602 |
A | ALA12 |
A | GLN15 |
A | ASP98 |
A | ALA99 |
A | ALA100 |
A | ASN101 |
A | SER140 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 502 |
Chain | Residue |
A | ASP69 |
A | GLU71 |
A | GTP501 |
A | HOH629 |
B | ASN247 |
B | HOH602 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CA A 503 |
Chain | Residue |
A | ASP39 |
A | THR41 |
A | GLY44 |
A | GLU55 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue GDP B 501 |
Chain | Residue |
B | GLY10 |
B | GLN11 |
B | CYS12 |
B | GLN15 |
B | SER138 |
B | GLY141 |
B | GLY142 |
B | THR143 |
B | GLY144 |
B | VAL175 |
B | GLU181 |
B | ASN204 |
B | TYR222 |
B | ASN226 |
B | MG502 |
B | HOH604 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue MG B 502 |
Chain | Residue |
B | GLN11 |
B | ASP177 |
B | GDP501 |
C | HOH632 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue MES B 503 |
Chain | Residue |
B | ASP161 |
B | ARG162 |
B | ASN195 |
B | THR196 |
B | ASP197 |
B | ARG251 |
site_id | AC7 |
Number of Residues | 18 |
Details | binding site for residue PN6 B 504 |
Chain | Residue |
A | THR179 |
A | HOH604 |
B | TYR50 |
B | ASN165 |
B | GLU198 |
B | TYR200 |
B | VAL236 |
B | THR237 |
B | CYS239 |
B | LEU240 |
B | LEU250 |
B | LEU253 |
B | MET257 |
B | ALA314 |
B | ALA315 |
B | ILE316 |
B | ILE368 |
B | HOH619 |
site_id | AC8 |
Number of Residues | 24 |
Details | binding site for residue GTP C 501 |
Chain | Residue |
C | HOH622 |
C | HOH626 |
D | LYS252 |
C | GLY10 |
C | GLN11 |
C | ALA12 |
C | GLN15 |
C | ASP98 |
C | ALA99 |
C | ALA100 |
C | ASN101 |
C | SER140 |
C | GLY143 |
C | GLY144 |
C | THR145 |
C | GLY146 |
C | SER178 |
C | GLU183 |
C | ASN206 |
C | TYR224 |
C | ASN228 |
C | ILE231 |
C | MG502 |
C | HOH621 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue MG C 502 |
Chain | Residue |
C | GLU71 |
C | GTP501 |
C | HOH621 |
C | HOH626 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue CA C 503 |
Chain | Residue |
C | ASP39 |
C | THR41 |
C | GLY44 |
C | GLU55 |
site_id | AD2 |
Number of Residues | 16 |
Details | binding site for residue GDP D 501 |
Chain | Residue |
D | GLY10 |
D | GLN11 |
D | CYS12 |
D | GLN15 |
D | SER138 |
D | GLY141 |
D | GLY142 |
D | THR143 |
D | GLY144 |
D | SER176 |
D | GLU181 |
D | ASN204 |
D | TYR222 |
D | ASN226 |
D | HOH1202 |
D | HOH1208 |
site_id | AD3 |
Number of Residues | 18 |
Details | binding site for residue PN6 D 502 |
Chain | Residue |
D | GLN134 |
D | ASN165 |
D | PHE167 |
D | GLU198 |
D | TYR200 |
D | VAL236 |
D | THR237 |
D | CYS239 |
D | LEU240 |
D | LEU246 |
D | LEU253 |
D | MET257 |
D | ALA314 |
D | ALA315 |
D | ILE316 |
D | ALA352 |
D | ILE368 |
D | HOH1209 |
site_id | AD4 |
Number of Residues | 15 |
Details | binding site for residue ACP F 401 |
Chain | Residue |
F | LYS74 |
F | GLN183 |
F | LYS184 |
F | LEU186 |
F | LYS198 |
F | ASP200 |
F | ARG202 |
F | ARG222 |
F | HIS239 |
F | THR241 |
F | ASN242 |
F | ASP318 |
F | ILE330 |
F | GLU331 |
F | ASN333 |
Functional Information from PROSITE/UniProt
site_id | PS00227 |
Number of Residues | 7 |
Details | TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG |
Chain | Residue | Details |
B | GLY140-GLY146 | |
A | GLY142-GLY148 |
site_id | PS00228 |
Number of Residues | 4 |
Details | TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI |
Chain | Residue | Details |
B | MET1-ILE4 |
site_id | PS00563 |
Number of Residues | 10 |
Details | STATHMIN_1 Stathmin family signature 1. PRRRDpSLEE |
Chain | Residue | Details |
E | PRO40-GLU49 |
site_id | PS01041 |
Number of Residues | 10 |
Details | STATHMIN_2 Stathmin family signature 2. AEKREHEREV |
Chain | Residue | Details |
E | ALA73-VAL82 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
Chain | Residue | Details |
E | SER46 |