5CA1
Crystal structure of T2R-TTL-Nocodazole complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005200 | molecular_function | structural constituent of cytoskeleton |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005874 | cellular_component | microtubule |
| A | 0007010 | biological_process | cytoskeleton organization |
| A | 0007017 | biological_process | microtubule-based process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000226 | biological_process | microtubule cytoskeleton organization |
| B | 0000278 | biological_process | mitotic cell cycle |
| B | 0001764 | biological_process | neuron migration |
| B | 0003924 | molecular_function | GTPase activity |
| B | 0005200 | molecular_function | structural constituent of cytoskeleton |
| B | 0005509 | molecular_function | calcium ion binding |
| 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 | 0031115 | biological_process | negative regulation of microtubule polymerization |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005200 | molecular_function | structural constituent of cytoskeleton |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0005874 | cellular_component | microtubule |
| C | 0007010 | biological_process | cytoskeleton organization |
| C | 0007017 | biological_process | microtubule-based process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000226 | biological_process | microtubule cytoskeleton organization |
| D | 0000278 | biological_process | mitotic cell cycle |
| D | 0001764 | biological_process | neuron migration |
| D | 0003924 | molecular_function | GTPase activity |
| D | 0005200 | molecular_function | structural constituent of cytoskeleton |
| D | 0005509 | molecular_function | calcium ion binding |
| 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 | 0031115 | biological_process | negative regulation of microtubule polymerization |
| 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 | 28 |
| Details | binding site for residue GTP A 501 |
| Chain | Residue |
| A | GLY10 |
| A | GLY143 |
| A | GLY144 |
| A | THR145 |
| A | GLY146 |
| A | VAL177 |
| A | SER178 |
| A | GLU183 |
| A | ASN206 |
| A | TYR224 |
| A | ASN228 |
| A | GLN11 |
| A | ILE231 |
| A | MG502 |
| A | HOH611 |
| A | HOH625 |
| A | HOH627 |
| A | HOH640 |
| A | HOH656 |
| A | HOH689 |
| B | LYS252 |
| 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 | GLU71 |
| A | GTP501 |
| A | HOH611 |
| A | HOH625 |
| A | HOH640 |
| A | HOH689 |
| 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 | 5 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | PRO274 |
| A | VAL275 |
| A | ASN300 |
| A | HOH638 |
| A | HOH651 |
| site_id | AC5 |
| Number of Residues | 20 |
| 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 | ASP177 |
| B | GLU181 |
| B | ASN204 |
| B | TYR222 |
| B | ASN226 |
| B | MG502 |
| B | HOH606 |
| B | HOH620 |
| B | HOH622 |
| B | HOH659 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | GLN11 |
| B | ASP177 |
| B | GDP501 |
| B | HOH617 |
| B | HOH659 |
| C | HOH610 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue MES B 503 |
| Chain | Residue |
| A | HOH676 |
| B | ARG156 |
| B | ASP161 |
| B | ARG162 |
| B | ILE163 |
| B | ASN195 |
| B | ASP197 |
| B | ARG251 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | binding site for residue NZO B 504 |
| Chain | Residue |
| B | TYR50 |
| B | GLN134 |
| B | ASN165 |
| B | GLU198 |
| B | TYR200 |
| B | VAL236 |
| B | THR237 |
| B | CYS239 |
| B | LEU240 |
| B | LEU246 |
| B | LEU250 |
| B | ALA315 |
| B | ILE316 |
| B | LYS350 |
| B | THR351 |
| B | ALA352 |
| site_id | AC9 |
| Number of Residues | 26 |
| Details | binding site for residue GTP C 501 |
| Chain | Residue |
| C | ALA100 |
| C | ASN101 |
| C | SER140 |
| C | GLY143 |
| C | GLY144 |
| C | THR145 |
| C | GLY146 |
| C | VAL177 |
| C | GLU183 |
| C | ASN206 |
| C | TYR224 |
| C | ASN228 |
| C | ILE231 |
| C | MG502 |
| C | HOH635 |
| C | HOH648 |
| C | HOH650 |
| C | HOH652 |
| C | HOH676 |
| D | LYS252 |
| C | GLY10 |
| C | GLN11 |
| C | ALA12 |
| C | GLN15 |
| C | ASP98 |
| C | ALA99 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 502 |
| Chain | Residue |
| C | GTP501 |
| C | HOH615 |
| C | HOH650 |
| C | HOH652 |
| C | HOH676 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue CA C 503 |
| Chain | Residue |
| C | ASP39 |
| C | THR41 |
| C | GLY44 |
| C | GLU55 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for residue GDP D 501 |
| Chain | Residue |
| D | GLY10 |
| D | GLN11 |
| D | CYS12 |
| D | SER138 |
| D | GLY141 |
| D | GLY142 |
| D | THR143 |
| D | GLY144 |
| D | VAL175 |
| D | SER176 |
| D | GLU181 |
| D | ASN204 |
| D | TYR222 |
| D | ASN226 |
| D | HOH626 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue MES D 502 |
| Chain | Residue |
| C | TRP407 |
| D | ARG156 |
| D | PRO160 |
| D | ASP161 |
| D | ARG162 |
| D | ASN195 |
| D | ASP197 |
| D | ARG251 |
| D | HOH609 |
| site_id | AD5 |
| Number of Residues | 15 |
| Details | binding site for residue NZO D 503 |
| Chain | Residue |
| D | GLN134 |
| D | ASN165 |
| D | GLU198 |
| D | TYR200 |
| D | VAL236 |
| D | CYS239 |
| D | LEU240 |
| D | LEU246 |
| D | LEU253 |
| D | ALA315 |
| D | ILE316 |
| D | LYS350 |
| D | THR351 |
| D | ALA352 |
| D | HOH616 |
| site_id | AD6 |
| Number of Residues | 16 |
| Details | binding site for residue ACP F 401 |
| Chain | Residue |
| F | LYS74 |
| F | GLN183 |
| F | LYS184 |
| F | TYR185 |
| F | LEU186 |
| F | LYS198 |
| F | ASP200 |
| F | ARG202 |
| F | ARG222 |
| F | LEU240 |
| 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 |
| A | GLY142-GLY148 | |
| B | GLY140-GLY146 |
| 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_FI9 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | Motif: {"description":"MREI motif","evidences":[{"source":"UniProtKB","id":"P07437","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
