6TIY
DROSOPHILA GMPCPP-TUBULIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000226 | biological_process | microtubule cytoskeleton organization |
| A | 0000235 | cellular_component | astral microtubule |
| A | 0000278 | biological_process | mitotic cell cycle |
| A | 0005200 | molecular_function | structural constituent of cytoskeleton |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005813 | cellular_component | centrosome |
| A | 0005819 | cellular_component | spindle |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005874 | cellular_component | microtubule |
| A | 0007017 | biological_process | microtubule-based process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0032418 | biological_process | lysosome localization |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048471 | cellular_component | perinuclear region of cytoplasm |
| B | 0000166 | molecular_function | nucleotide 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 | 0000166 | molecular_function | nucleotide binding |
| C | 0000226 | biological_process | microtubule cytoskeleton organization |
| C | 0000235 | cellular_component | astral microtubule |
| C | 0000278 | biological_process | mitotic cell cycle |
| C | 0005200 | molecular_function | structural constituent of cytoskeleton |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005813 | cellular_component | centrosome |
| C | 0005819 | cellular_component | spindle |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0005874 | cellular_component | microtubule |
| C | 0007017 | biological_process | microtubule-based process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0032418 | biological_process | lysosome localization |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048471 | cellular_component | perinuclear region of cytoplasm |
| D | 0000166 | molecular_function | nucleotide 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 |
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 | GLY144 |
| A | THR145 |
| A | GLY146 |
| A | VAL177 |
| A | THR179 |
| A | GLU183 |
| A | ASN206 |
| A | TYR224 |
| A | ASN228 |
| A | ILE231 |
| A | GLN11 |
| A | MG502 |
| A | HOH616 |
| A | HOH620 |
| A | HOH656 |
| A | HOH657 |
| A | HOH662 |
| A | HOH675 |
| A | HOH698 |
| B | LYS252 |
| A | ALA12 |
| A | GLN15 |
| A | ASP98 |
| A | ALA99 |
| A | ASN101 |
| A | SER140 |
| A | GLY143 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | GTP501 |
| A | HOH616 |
| A | HOH656 |
| A | HOH662 |
| A | HOH698 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | PRO175 |
| A | LYS394 |
| A | HOH696 |
| A | HOH701 |
| B | ASN347 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | ASN216 |
| A | ALA294 |
| A | HOH652 |
| D | LYS122 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | ARG308 |
| A | ARG339 |
| A | THR340 |
| A | HOH660 |
| A | HOH677 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 506 |
| Chain | Residue |
| A | GLY410 |
| A | GLU411 |
| E | ARG61 |
| E | GLN64 |
| E | GLU65 |
| site_id | AC7 |
| Number of Residues | 25 |
| Details | binding site for residue G2P B 501 |
| Chain | Residue |
| B | GLY10 |
| B | GLN11 |
| B | CYS12 |
| B | GLN15 |
| B | ALA97 |
| B | ASN99 |
| 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 | MG502 |
| B | HOH609 |
| B | HOH631 |
| B | HOH633 |
| B | HOH649 |
| B | HOH668 |
| B | HOH675 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | G2P501 |
| B | HOH614 |
| B | HOH631 |
| B | HOH668 |
| B | HOH679 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 503 |
| Chain | Residue |
| B | THR221 |
| B | GLY223 |
| B | ARG276 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | LYS216 |
| B | LEU217 |
| B | THR218 |
| B | THR219 |
| C | LYS326 |
| site_id | AD2 |
| Number of Residues | 29 |
| Details | binding site for residue GTP C 501 |
| Chain | Residue |
| C | GLY143 |
| C | GLY144 |
| C | THR145 |
| C | GLY146 |
| C | VAL177 |
| C | THR179 |
| C | GLU183 |
| C | ASN206 |
| C | TYR224 |
| C | ASN228 |
| C | ILE231 |
| C | MG502 |
| C | HOH606 |
| C | HOH620 |
| C | HOH624 |
| C | HOH627 |
| C | HOH634 |
| C | HOH640 |
| C | HOH668 |
| D | LYS252 |
| C | GLY10 |
| C | GLN11 |
| C | ALA12 |
| C | GLN15 |
| C | ASP98 |
| C | ALA99 |
| C | ALA100 |
| C | ASN101 |
| C | SER140 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 502 |
| Chain | Residue |
| C | GTP501 |
| C | HOH624 |
| C | HOH627 |
| C | HOH634 |
| C | HOH668 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 C 503 |
| Chain | Residue |
| C | TYR262 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 504 |
| Chain | Residue |
| C | PRO175 |
| C | LYS394 |
| C | HOH612 |
| D | ASN347 |
| site_id | AD6 |
| Number of Residues | 29 |
| Details | binding site for residue G2P D 501 |
| Chain | Residue |
| D | GLY10 |
| D | GLN11 |
| D | CYS12 |
| D | GLN15 |
| D | ALA97 |
| D | GLY98 |
| D | ASN99 |
| D | SER138 |
| D | GLY141 |
| D | GLY142 |
| D | THR143 |
| D | GLY144 |
| D | PRO171 |
| D | VAL175 |
| D | SER176 |
| D | GLU181 |
| D | ASN204 |
| D | TYR222 |
| D | ASN226 |
| D | MG502 |
| D | HOH603 |
| D | HOH604 |
| D | HOH611 |
| D | HOH619 |
| D | HOH624 |
| D | HOH647 |
| D | HOH655 |
| D | HOH665 |
| D | HOH672 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 502 |
| Chain | Residue |
| D | G2P501 |
| D | HOH603 |
| D | HOH655 |
| D | HOH665 |
| D | HOH677 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 D 503 |
| Chain | Residue |
| D | THR221 |
| D | ARG276 |
| D | ALA393 |
| D | PHE394 |
| D | HOH620 |
| D | HOH636 |
| D | HOH649 |
| D | HOH667 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 D 504 |
| Chain | Residue |
| D | LYS19 |
| D | HIS227 |
| D | SER230 |
| D | ARG276 |
| D | ARG359 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 505 |
| Chain | Residue |
| D | ALA271 |
| D | PRO272 |
| D | LEU273 |
| D | LEU284 |
| D | GLN292 |
| D | ASN298 |
| D | HOH663 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 E 201 |
| Chain | Residue |
| E | HIS115 |
| E | ALA118 |
| E | ARG122 |
| E | HOH301 |
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_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P68363","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q13509","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18327897","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 21 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 99 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |






