5XHC
Crystal structure of T2R-TTL-PO10 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 | 0005737 | cellular_component | cytoplasm |
| E | 0005794 | cellular_component | Golgi apparatus |
| E | 0007019 | biological_process | microtubule depolymerization |
| E | 0015631 | molecular_function | tubulin binding |
| E | 0030424 | cellular_component | axon |
| E | 0030426 | cellular_component | growth cone |
| E | 0031110 | biological_process | regulation of microtubule polymerization or depolymerization |
| E | 0031175 | biological_process | neuron projection development |
| E | 0042995 | cellular_component | cell projection |
| E | 0043005 | cellular_component | neuron projection |
| F | 0036211 | biological_process | protein modification process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 26 |
| Details | binding site for residue GTP A 501 |
| Chain | Residue |
| A | GLY10 |
| A | GLY143 |
| A | GLY144 |
| A | THR145 |
| A | GLY146 |
| A | VAL177 |
| A | GLU183 |
| A | ASN206 |
| A | TYR224 |
| A | ASN228 |
| A | ILE231 |
| A | GLN11 |
| A | HOH601 |
| A | HOH604 |
| A | HOH606 |
| A | HOH612 |
| B | LYS252 |
| B | MG501 |
| B | HOH604 |
| A | ALA12 |
| A | GLN15 |
| A | ASP98 |
| A | ALA99 |
| A | ALA100 |
| A | ASN101 |
| A | SER140 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | ASP39 |
| A | THR41 |
| A | GLY44 |
| A | GLU55 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 501 |
| Chain | Residue |
| A | GTP501 |
| A | HOH606 |
| A | HOH612 |
| B | LYS252 |
| B | HOH604 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | binding site for residue GDP B 502 |
| Chain | Residue |
| B | GLY10 |
| B | GLN11 |
| B | CYS12 |
| B | GLN15 |
| B | SER138 |
| B | GLY141 |
| B | GLY142 |
| B | THR143 |
| B | GLY144 |
| B | PRO171 |
| B | VAL175 |
| B | ASP177 |
| B | GLU181 |
| B | ASN204 |
| B | TYR222 |
| B | ASN226 |
| B | MG503 |
| B | HOH601 |
| B | HOH602 |
| B | HOH606 |
| B | HOH607 |
| B | HOH608 |
| B | HOH613 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 503 |
| Chain | Residue |
| B | GLN11 |
| B | ASP177 |
| B | GDP502 |
| B | HOH607 |
| B | HOH618 |
| C | HOH635 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | binding site for residue MES B 504 |
| Chain | Residue |
| B | ARG156 |
| B | PRO160 |
| B | ASP161 |
| B | ARG162 |
| B | ILE163 |
| B | ASN195 |
| B | ASP197 |
| B | ARG251 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | binding site for residue 87U B 505 |
| Chain | Residue |
| A | THR179 |
| B | GLN134 |
| B | THR136 |
| B | ASN165 |
| B | PHE167 |
| B | GLU198 |
| B | TYR200 |
| B | MET233 |
| B | VAL236 |
| B | THR237 |
| B | CYS239 |
| B | LEU240 |
| B | LEU250 |
| B | LEU253 |
| B | ALA314 |
| B | ALA315 |
| B | ILE368 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue CA B 506 |
| Chain | Residue |
| B | GLU111 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MES B 507 |
| Chain | Residue |
| B | PHE294 |
| B | ASP295 |
| B | SER296 |
| B | ARG306 |
| B | ASN337 |
| site_id | AD1 |
| Number of Residues | 26 |
| Details | binding site for residue GTP C 501 |
| Chain | Residue |
| C | ASP69 |
| C | ASP98 |
| C | ALA99 |
| 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 | HOH605 |
| C | HOH609 |
| C | HOH629 |
| C | HOH637 |
| D | LYS252 |
| C | GLY10 |
| C | GLN11 |
| C | ALA12 |
| C | GLN15 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 502 |
| Chain | Residue |
| C | GTP501 |
| C | HOH605 |
| C | HOH611 |
| C | HOH629 |
| C | HOH637 |
| D | LYS252 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue CA C 503 |
| Chain | Residue |
| C | ASP39 |
| C | THR41 |
| C | GLY44 |
| C | ASP47 |
| C | GLU55 |
| site_id | AD4 |
| Number of Residues | 18 |
| Details | binding site for residue GTP D 501 |
| Chain | Residue |
| D | GLY10 |
| D | GLN11 |
| D | CYS12 |
| D | ALA97 |
| D | GLY98 |
| D | ASN99 |
| D | SER138 |
| D | GLY141 |
| D | GLY142 |
| D | THR143 |
| D | GLY144 |
| D | VAL175 |
| D | SER176 |
| D | GLU181 |
| D | ASN204 |
| D | TYR222 |
| D | ASN226 |
| D | MG502 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue MG D 502 |
| Chain | Residue |
| D | GTP501 |
| site_id | AD6 |
| Number of Residues | 17 |
| Details | binding site for residue ACP F 401 |
| Chain | Residue |
| F | LYS74 |
| F | LYS150 |
| F | GLN183 |
| F | LYS184 |
| F | TYR185 |
| F | LEU186 |
| F | LYS198 |
| F | ASP200 |
| F | ARG202 |
| F | ARG222 |
| F | THR241 |
| F | ASN242 |
| F | ASP318 |
| F | MET320 |
| 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 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000250 |
| Chain | Residue | Details |
| E | CYS-24 | |
| E | CYS-22 |
