Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005200 | molecular_function | structural constituent of cytoskeleton |
A | 0005525 | molecular_function | GTP binding |
A | 0005874 | cellular_component | microtubule |
A | 0007017 | biological_process | microtubule-based process |
B | 0003924 | molecular_function | GTPase activity |
B | 0005200 | molecular_function | structural constituent of cytoskeleton |
B | 0005525 | molecular_function | GTP binding |
B | 0005874 | cellular_component | microtubule |
B | 0007017 | biological_process | microtubule-based process |
C | 0005200 | molecular_function | structural constituent of cytoskeleton |
C | 0005525 | molecular_function | GTP binding |
C | 0005874 | cellular_component | microtubule |
C | 0007017 | biological_process | microtubule-based process |
D | 0003924 | molecular_function | GTPase activity |
D | 0005200 | molecular_function | structural constituent of cytoskeleton |
D | 0005525 | molecular_function | GTP binding |
D | 0005874 | cellular_component | microtubule |
D | 0007017 | biological_process | microtubule-based process |
E | 0031110 | biological_process | regulation of microtubule polymerization or depolymerization |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 501 |
Chain | Residue |
A | PRO175 |
A | LYS394 |
B | ASN349 |
site_id | AC2 |
Number of Residues | 27 |
Details | binding site for residue GTP A 502 |
Chain | Residue |
A | ASN101 |
A | SER140 |
A | GLY143 |
A | GLY144 |
A | THR145 |
A | GLY146 |
A | VAL177 |
A | SER178 |
A | GLU183 |
A | ASN206 |
A | TYR224 |
A | ASN228 |
A | ILE231 |
A | MG503 |
A | HOH602 |
A | HOH605 |
A | HOH607 |
A | HOH608 |
A | HOH609 |
A | HOH616 |
B | LYS254 |
A | GLY10 |
A | GLN11 |
A | ALA12 |
A | GLN15 |
A | ASP98 |
A | ALA99 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MG A 503 |
Chain | Residue |
A | GTP502 |
A | HOH602 |
A | HOH605 |
A | HOH607 |
A | HOH608 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 501 |
Chain | Residue |
B | LEU219 |
B | THR220 |
B | THR221 |
C | LYS326 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue SO4 B 502 |
Chain | Residue |
B | THR223 |
B | GLY225 |
B | ARG278 |
site_id | AC6 |
Number of Residues | 21 |
Details | binding site for residue GDP B 503 |
Chain | Residue |
B | GLY10 |
B | GLN11 |
B | CYS12 |
B | GLN15 |
B | SER140 |
B | GLY143 |
B | GLY144 |
B | THR145 |
B | GLY146 |
B | PRO173 |
B | VAL177 |
B | ASP179 |
B | GLU183 |
B | ASN206 |
B | TYR224 |
B | ASN228 |
B | HOH602 |
B | HOH605 |
B | HOH606 |
B | HOH609 |
B | HOH612 |
site_id | AC7 |
Number of Residues | 16 |
Details | binding site for residue N9B B 504 |
Chain | Residue |
A | ALA180 |
A | VAL181 |
B | VAL238 |
B | CYS241 |
B | LEU242 |
B | LEU248 |
B | ASN249 |
B | ALA250 |
B | ASN258 |
B | MET259 |
B | VAL315 |
B | ALA316 |
B | ASN350 |
B | LYS352 |
B | ILE378 |
B | HOH611 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue SO4 C 501 |
Chain | Residue |
C | ARG215 |
C | LYS304 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue SO4 C 502 |
Chain | Residue |
C | ARG390 |
C | LYS394 |
site_id | AD1 |
Number of Residues | 28 |
Details | binding site for residue GTP C 503 |
Chain | Residue |
C | ASN206 |
C | TYR224 |
C | ASN228 |
C | ILE231 |
C | HOH606 |
C | HOH608 |
C | HOH611 |
C | HOH612 |
C | HOH614 |
C | HOH617 |
D | LYS254 |
D | MG501 |
C | GLY10 |
C | GLN11 |
C | ALA12 |
C | GLN15 |
C | ASP98 |
C | ALA99 |
C | ASN101 |
C | SER140 |
C | GLY143 |
C | GLY144 |
C | THR145 |
C | GLY146 |
C | ILE171 |
C | VAL177 |
C | SER178 |
C | GLU183 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue MG D 501 |
Chain | Residue |
C | GTP503 |
C | HOH611 |
C | HOH614 |
D | LYS254 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue SO4 D 502 |
Chain | Residue |
D | THR223 |
D | ARG278 |
D | PHE404 |
D | HIS406 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue SO4 D 503 |
Chain | Residue |
D | LYS19 |
D | HIS229 |
D | ARG278 |
site_id | AD5 |
Number of Residues | 24 |
Details | binding site for residue GDP D 504 |
Chain | Residue |
D | GLY10 |
D | GLN11 |
D | CYS12 |
D | GLN15 |
D | SER140 |
D | GLY143 |
D | GLY144 |
D | THR145 |
D | GLY146 |
D | PRO173 |
D | VAL177 |
D | SER178 |
D | ASP179 |
D | GLU183 |
D | ASN206 |
D | TYR224 |
D | ASN228 |
D | HOH604 |
D | HOH605 |
D | HOH607 |
D | HOH610 |
D | HOH614 |
D | HOH619 |
D | HOH624 |
site_id | AD6 |
Number of Residues | 16 |
Details | binding site for residue N9B D 505 |
Chain | Residue |
C | ASN101 |
C | ALA180 |
C | VAL181 |
D | CYS241 |
D | LEU242 |
D | LEU248 |
D | ALA250 |
D | ASP251 |
D | LEU255 |
D | ASN258 |
D | MET259 |
D | VAL315 |
D | ALA316 |
D | ASN350 |
D | LYS352 |
D | ILE378 |
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 | 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
Chain | Residue | Details |
E | SER19 | |