4I4T
Crystal structure of tubulin-RB3-TTL-Zampanolide 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 | 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 | 0007017 | biological_process | microtubule-based process |
| A | 0015630 | cellular_component | microtubule cytoskeleton |
| 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 | 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 |
| C | 0000226 | biological_process | microtubule cytoskeleton organization |
| C | 0000278 | biological_process | mitotic cell cycle |
| C | 0003924 | molecular_function | GTPase activity |
| C | 0005200 | molecular_function | structural constituent of cytoskeleton |
| C | 0005525 | molecular_function | GTP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0005874 | cellular_component | microtubule |
| C | 0007017 | biological_process | microtubule-based process |
| C | 0015630 | cellular_component | microtubule cytoskeleton |
| 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 | 0007399 | biological_process | nervous system development |
| D | 0015630 | cellular_component | microtubule cytoskeleton |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0046982 | molecular_function | protein heterodimerization activity |
| D | 1902669 | biological_process | positive regulation of axon guidance |
| E | 0031110 | biological_process | regulation of microtubule polymerization or depolymerization |
| F | 0036211 | biological_process | protein modification process |
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 | GLU183 |
| A | ASN206 |
| A | TYR224 |
| A | ASN228 |
| A | ILE231 |
| A | MG502 |
| A | GLN11 |
| A | HOH601 |
| A | HOH602 |
| A | HOH613 |
| A | HOH644 |
| A | HOH681 |
| A | HOH683 |
| A | HOH700 |
| A | HOH872 |
| B | LYS254 |
| 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 | HOH602 |
| A | HOH681 |
| A | HOH683 |
| A | HOH872 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 503 |
| Chain | Residue |
| A | ASP39 |
| A | THR41 |
| A | GLY44 |
| A | GLU55 |
| A | HOH702 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 504 |
| Chain | Residue |
| A | TYR161 |
| A | GLY162 |
| A | LYS163 |
| A | LYS164 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 505 |
| Chain | Residue |
| A | GOL507 |
| A | HOH712 |
| A | HOH900 |
| A | HOH916 |
| E | HOH258 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 506 |
| Chain | Residue |
| A | ARG105 |
| A | THR109 |
| A | GLY410 |
| A | GLU411 |
| A | HOH863 |
| A | HOH910 |
| B | MES507 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 507 |
| Chain | Residue |
| A | GLY162 |
| A | LYS163 |
| A | LYS164 |
| A | SER165 |
| A | ASP199 |
| A | CA505 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 508 |
| Chain | Residue |
| A | ASN216 |
| A | PRO274 |
| A | VAL275 |
| A | ASN300 |
| A | HOH637 |
| A | HOH694 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE GDP B 501 |
| 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 | MG502 |
| B | HOH602 |
| B | HOH603 |
| B | HOH607 |
| B | HOH680 |
| B | HOH681 |
| B | HOH682 |
| B | HOH686 |
| B | HOH695 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 502 |
| Chain | Residue |
| B | GLN11 |
| B | GDP501 |
| B | HOH623 |
| B | HOH694 |
| B | HOH695 |
| B | HOH791 |
| C | HOH794 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 503 |
| Chain | Residue |
| B | HOH677 |
| B | HOH729 |
| B | HOH741 |
| B | HOH833 |
| B | GLU113 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 504 |
| Chain | Residue |
| B | ASP297 |
| B | SER298 |
| B | ARG308 |
| B | GOL505 |
| B | HOH738 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 505 |
| Chain | Residue |
| B | PHE296 |
| B | ARG308 |
| B | VAL335 |
| B | ASN339 |
| B | GOL504 |
| B | HOH802 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TYR B 506 |
| Chain | Residue |
| B | ARG401 |
| B | HOH696 |
| B | HOH723 |
| B | HOH798 |
| C | TYR262 |
| C | ASP431 |
| C | VAL435 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES B 507 |
| Chain | Residue |
| A | GOL506 |
| B | ARG158 |
| B | PRO162 |
| B | ASP163 |
| B | ARG164 |
| B | ASN197 |
| B | ASP199 |
| B | ARG253 |
| site_id | BC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE GTP C 501 |
| Chain | Residue |
| C | GLY10 |
| C | GLN11 |
| C | ALA12 |
| C | GLN15 |
| 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 | HOH676 |
| C | HOH771 |
| C | HOH773 |
| C | HOH779 |
| C | HOH791 |
| C | HOH839 |
| C | HOH951 |
| D | LYS254 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 502 |
| Chain | Residue |
| C | GTP501 |
| C | HOH771 |
| C | HOH791 |
| C | HOH839 |
| C | HOH949 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 503 |
| Chain | Residue |
| C | ASP39 |
| C | THR41 |
| C | GLY44 |
| C | GLU55 |
| C | HOH792 |
| site_id | CC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE GDP D 501 |
| Chain | Residue |
| D | GLY10 |
| D | GLN11 |
| D | CYS12 |
| D | GLN15 |
| D | SER140 |
| D | GLY143 |
| D | GLY144 |
| D | THR145 |
| D | GLY146 |
| D | VAL177 |
| D | GLU183 |
| D | ASN206 |
| D | TYR224 |
| D | ASN228 |
| D | MG502 |
| D | HOH605 |
| D | HOH620 |
| D | HOH661 |
| D | HOH677 |
| D | HOH684 |
| D | HOH751 |
| D | HOH809 |
| D | HOH829 |
| D | HOH845 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 502 |
| Chain | Residue |
| D | GLN11 |
| D | ASP179 |
| D | GDP501 |
| D | HOH784 |
| D | HOH809 |
| D | HOH829 |
| site_id | CC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ZPN D 503 |
| Chain | Residue |
| D | LEU217 |
| D | HIS229 |
| D | ALA233 |
| D | PRO274 |
| D | THR276 |
| D | ARG278 |
| D | GLN281 |
| D | ARG284 |
| D | PRO360 |
| D | HOH686 |
| D | HOH708 |
| D | HOH743 |
| D | HOH837 |
| site_id | CC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG F 701 |
| Chain | Residue |
| F | ASP318 |
| F | ACP703 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 702 |
| Chain | Residue |
| F | GLU331 |
| F | ASN333 |
| F | ACP703 |
| F | HOH802 |
| F | HOH936 |
| F | HOH955 |
| site_id | CC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ACP F 703 |
| Chain | Residue |
| A | GLU450 |
| F | LYS74 |
| F | LYS150 |
| F | GLN183 |
| F | LYS184 |
| F | TYR185 |
| F | LEU186 |
| F | LYS198 |
| F | ASP200 |
| F | ARG202 |
| F | HIS239 |
| F | LEU240 |
| F | THR241 |
| F | ASN242 |
| F | ASP318 |
| F | GLU331 |
| F | ASN333 |
| F | MG701 |
| F | MG702 |
| F | HOH979 |
| F | HOH981 |
| F | HOH983 |
| F | HOH1003 |
| site_id | CC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL F 704 |
| Chain | Residue |
| F | TYR211 |
| F | ARG292 |
| F | MET296 |
| F | LEU378 |
| F | HIS379 |
| F | HIS380 |
| F | HOH812 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL F 705 |
| Chain | Residue |
| D | ARG311 |
| D | SER341 |
| F | ARG292 |
| F | LYS377 |
| F | LEU378 |
| F | HIS379 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903 |
| Chain | Residue | Details |
| E | SER46 | |
| D | GLY144 | |
| D | THR145 | |
| D | GLY146 | |
| D | ASN206 | |
| D | ASN228 | |
| B | SER140 | |
| B | GLY144 | |
| B | THR145 | |
| B | GLY146 | |
| B | ASN206 | |
| B | ASN228 | |
| D | GLN11 | |
| D | SER140 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P68363 |
| Chain | Residue | Details |
| B | GLU71 | |
| C | GLU71 | |
| C | SER140 | |
| C | GLY144 | |
| C | THR145 | |
| C | THR179 | |
| C | ASN206 | |
| C | ASN228 | |
| D | GLU71 | |
| A | SER140 | |
| A | GLY144 | |
| A | THR145 | |
| A | THR179 | |
| A | ASN206 | |
| A | ASN228 | |
| C | GLN11 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P99024 |
| Chain | Residue | Details |
| B | SER40 | |
| D | SER40 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 |
| Chain | Residue | Details |
| B | THR57 | |
| D | THR57 | |
| C | SER48 | |
| C | SER232 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 |
| Chain | Residue | Details |
| B | LYS60 | |
| D | LYS60 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 |
| Chain | Residue | Details |
| B | SER174 | |
| D | SER174 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P07437 |
| Chain | Residue | Details |
| B | THR287 | |
| B | THR292 | |
| D | THR287 | |
| D | THR292 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 |
| Chain | Residue | Details |
| B | ARG320 | |
| D | ARG320 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: 5-glutamyl polyglutamate => ECO:0000250|UniProtKB:Q2T9S0 |
| Chain | Residue | Details |
| B | GLU448 | |
| D | GLU448 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 |
| Chain | Residue | Details |
| B | LYS60 | |
| D | LYS60 | |
| A | LYS370 | |
| C | LYS326 | |
| C | LYS370 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 |
| Chain | Residue | Details |
| B | LYS326 | |
| D | LYS326 |
