1JFF
Refined structure of alpha-beta tubulin from zinc-induced sheets stabilized with taxol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000226 | biological_process | microtubule cytoskeleton organization |
| A | 0000278 | biological_process | mitotic cell cycle |
| A | 0003725 | molecular_function | double-stranded RNA binding |
| A | 0003924 | molecular_function | GTPase activity |
| A | 0005200 | molecular_function | structural constituent of cytoskeleton |
| A | 0005525 | molecular_function | GTP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0005874 | cellular_component | microtubule |
| A | 0005881 | cellular_component | cytoplasmic microtubule |
| A | 0007017 | biological_process | microtubule-based process |
| A | 0015630 | cellular_component | microtubule cytoskeleton |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0031625 | molecular_function | ubiquitin protein ligase binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071353 | biological_process | cellular response to interleukin-4 |
| 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 | 0007399 | biological_process | nervous system development |
| B | 0015630 | cellular_component | microtubule cytoskeleton |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| B | 1902669 | biological_process | positive regulation of axon guidance |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ZN A 900 |
| Chain | Residue |
| A | HIS283 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 501 |
| Chain | Residue |
| A | GLN11 |
| A | GLU71 |
| A | GTP500 |
| site_id | AC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GTP A 500 |
| Chain | Residue |
| A | ALA100 |
| A | ASN101 |
| A | SER140 |
| A | GLY143 |
| A | GLY144 |
| A | THR145 |
| A | GLY146 |
| A | ILE171 |
| A | GLU183 |
| A | ASN206 |
| A | TYR224 |
| A | ASN228 |
| A | MG501 |
| B | LEU248 |
| B | LYS254 |
| A | GLY10 |
| A | GLN11 |
| A | ALA12 |
| A | GLN15 |
| A | ALA99 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE GDP B 600 |
| Chain | Residue |
| B | GLY10 |
| B | GLN11 |
| B | CYS12 |
| B | GLN15 |
| B | SER140 |
| B | GLY142 |
| B | GLY144 |
| B | THR145 |
| B | GLY146 |
| B | ASP179 |
| B | ASN206 |
| B | TYR224 |
| B | ASN228 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE TA1 B 601 |
| Chain | Residue |
| B | VAL23 |
| B | ASP26 |
| B | GLU27 |
| B | HIS229 |
| B | LEU230 |
| B | ALA233 |
| B | SER236 |
| B | PHE272 |
| B | PRO274 |
| B | LEU275 |
| B | THR276 |
| B | ARG278 |
| B | PRO360 |
| B | ARG369 |
| B | GLY370 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q13509 |
| Chain | Residue | Details |
| B | GLN11 | |
| B | SER140 | |
| B | GLY144 | |
| B | THR145 | |
| B | GLY146 | |
| B | ASN206 | |
| B | ASN228 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P68363 |
| Chain | Residue | Details |
| B | GLU71 | |
| A | GLU71 | |
| A | SER140 | |
| A | GLY144 | |
| A | THR145 | |
| A | THR179 | |
| A | ASN206 | |
| A | ASN228 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024 |
| Chain | Residue | Details |
| B | SER40 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 |
| Chain | Residue | Details |
| B | ALA57 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 |
| Chain | Residue | Details |
| B | LYS60 | |
| A | GLY232 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 |
| Chain | Residue | Details |
| B | SER174 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437 |
| Chain | Residue | Details |
| B | THR287 | |
| B | THR292 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 |
| Chain | Residue | Details |
| B | ARG320 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0 |
| Chain | Residue | Details |
| B | GLU448 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 |
| Chain | Residue | Details |
| B | LYS60 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 |
| Chain | Residue | Details |
| A | TYR451 | |
| B | LYS326 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 |
| Chain | Residue | Details |
| A | LYS326 | |
| A | LYS370 |
