6TIZ
DROSOPHILA GDP-TUBULIN Y222F MUTANT
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 | 30 |
Details | binding site for residue GTP A 501 |
Chain | Residue |
A | GLY10 |
A | GLY143 |
A | GLY144 |
A | THR145 |
A | GLY146 |
A | VAL177 |
A | THR179 |
A | GLU183 |
A | ASN206 |
A | TYR224 |
A | ASN228 |
A | GLN11 |
A | ILE231 |
A | MG502 |
A | HOH604 |
A | HOH633 |
A | HOH659 |
A | HOH669 |
A | HOH693 |
A | HOH705 |
A | HOH734 |
A | HOH738 |
A | ALA12 |
B | LYS252 |
A | GLN15 |
A | ASP98 |
A | ALA99 |
A | ALA100 |
A | ASN101 |
A | SER140 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 502 |
Chain | Residue |
A | GTP501 |
A | HOH604 |
A | HOH659 |
A | HOH669 |
A | HOH738 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | PRO175 |
A | LYS394 |
A | HOH723 |
B | ASN347 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 504 |
Chain | Residue |
A | ARG308 |
A | ARG339 |
A | THR340 |
A | ILE341 |
A | HOH605 |
A | HOH678 |
A | HOH748 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 505 |
Chain | Residue |
A | ASN216 |
A | LEU286 |
A | HOH625 |
A | HOH714 |
D | LYS122 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | ARG105 |
A | GLY410 |
A | GLU411 |
A | HOH697 |
E | ARG61 |
E | GLU65 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue GOL A 507 |
Chain | Residue |
A | VAL177 |
A | ARG221 |
A | THR223 |
A | TYR224 |
site_id | AC8 |
Number of Residues | 24 |
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 | PRO171 |
B | VAL175 |
B | ASP177 |
B | GLU181 |
B | ASN204 |
B | PHE222 |
B | ASN226 |
B | HOH618 |
B | HOH619 |
B | HOH621 |
B | HOH628 |
B | HOH629 |
B | HOH646 |
B | HOH655 |
B | HOH684 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
B | THR221 |
B | GLY223 |
B | ARG276 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 503 |
Chain | Residue |
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 | ASN101 |
C | SER140 |
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 | HOH607 |
C | HOH623 |
C | HOH626 |
C | HOH640 |
C | HOH656 |
C | HOH669 |
C | HOH692 |
D | LYS252 |
C | GLY10 |
C | GLN11 |
C | ALA12 |
C | GLN15 |
C | ASP98 |
C | ALA99 |
C | ALA100 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue MG C 502 |
Chain | Residue |
C | GTP501 |
C | HOH623 |
C | HOH626 |
C | HOH640 |
C | HOH692 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 503 |
Chain | Residue |
C | TYR262 |
C | ASP431 |
C | HOH627 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue SO4 C 504 |
Chain | Residue |
C | PRO175 |
C | LYS394 |
C | HOH648 |
D | ASN347 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 505 |
Chain | Residue |
C | ASP211 |
C | ARG215 |
C | LYS304 |
site_id | AD7 |
Number of Residues | 25 |
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 | PRO171 |
D | VAL175 |
D | SER176 |
D | ASP177 |
D | GLU181 |
D | ASN204 |
D | PHE222 |
D | ASN226 |
D | HOH607 |
D | HOH613 |
D | HOH624 |
D | HOH626 |
D | HOH630 |
D | HOH638 |
D | HOH701 |
D | HOH736 |
site_id | AD8 |
Number of Residues | 8 |
Details | binding site for residue SO4 D 502 |
Chain | Residue |
D | THR221 |
D | ARG276 |
D | ALA393 |
D | PHE394 |
D | HOH610 |
D | HOH637 |
D | HOH643 |
D | HOH710 |
site_id | AD9 |
Number of Residues | 6 |
Details | binding site for residue SO4 D 503 |
Chain | Residue |
D | LYS19 |
D | GLU22 |
D | HIS227 |
D | ARG276 |
D | ARG359 |
D | HOH661 |
site_id | AE1 |
Number of Residues | 3 |
Details | binding site for residue SO4 D 504 |
Chain | Residue |
D | HIS396 |
D | HOH674 |
D | HOH740 |
site_id | AE2 |
Number of Residues | 7 |
Details | binding site for residue SO4 D 505 |
Chain | Residue |
D | ALA271 |
D | PRO272 |
D | LEU273 |
D | LEU284 |
D | ASN298 |
D | HOH691 |
D | HOH717 |
site_id | AE3 |
Number of Residues | 4 |
Details | binding site for residue SO4 E 201 |
Chain | Residue |
E | HIS115 |
E | ALA118 |
E | ARG122 |
E | HOH310 |
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 | |
D | GLY142 | |
D | THR143 | |
D | GLY144 | |
D | ASN204 | |
D | ASN226 | |
B | SER138 | |
B | GLY142 | |
B | THR143 | |
B | GLY144 | |
B | ASN204 | |
B | ASN226 | |
D | GLN11 | |
D | SER138 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P68363 |
Chain | Residue | Details |
B | GLU69 | |
C | GLU71 | |
C | SER140 | |
C | GLY144 | |
C | THR145 | |
C | THR179 | |
C | ASN206 | |
C | ASN228 | |
D | GLU69 | |
A | SER140 | |
A | GLY144 | |
A | THR145 | |
A | THR179 | |
A | ASN206 | |
A | ASN228 | |
C | GLN11 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18327897 |
Chain | Residue | Details |
B | SER40 | |
B | SER339 | |
D | SER40 | |
D | SER339 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:36342916 |
Chain | Residue | Details |
A | ARG40 | |
C | ARG40 |