4IHJ
Crystal structure of tubulin-stathmin-TTL-ADP 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 | 29 |
| Details | BINDING SITE FOR RESIDUE GTP A 501 |
| Chain | Residue |
| A | GLY10 |
| A | GLY143 |
| A | GLY144 |
| A | THR145 |
| A | GLY146 |
| A | VAL177 |
| A | GLU183 |
| A | ASN206 |
| A | TYR224 |
| A | ASN228 |
| A | ILE231 |
| A | GLN11 |
| A | MG502 |
| A | HOH601 |
| A | HOH602 |
| A | HOH613 |
| A | HOH642 |
| A | HOH681 |
| A | HOH683 |
| A | HOH700 |
| A | HOH758 |
| B | LYS254 |
| A | ALA12 |
| 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 | HOH602 |
| A | HOH681 |
| A | HOH683 |
| A | HOH811 |
| 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 | 3 |
| Details | BINDING SITE FOR RESIDUE CA A 505 |
| Chain | Residue |
| A | HOH679 |
| A | HOH710 |
| E | ASP44 |
| site_id | AC6 |
| Number of Residues | 24 |
| 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 | HOH601 |
| B | HOH602 |
| B | HOH605 |
| B | HOH671 |
| B | HOH672 |
| B | HOH676 |
| B | HOH786 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 502 |
| Chain | Residue |
| B | GLN11 |
| B | GDP501 |
| B | HOH621 |
| B | HOH681 |
| B | HOH785 |
| B | HOH786 |
| C | HOH782 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 503 |
| Chain | Residue |
| B | GLU113 |
| B | HOH670 |
| B | HOH698 |
| B | HOH701 |
| C | GLU284 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES B 504 |
| Chain | Residue |
| B | ARG158 |
| B | PRO162 |
| B | ASP163 |
| B | ARG164 |
| B | MET166 |
| B | ASN197 |
| B | ASP199 |
| B | ARG253 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MES B 505 |
| Chain | Residue |
| B | HOH761 |
| B | PHE296 |
| B | ASP297 |
| B | SER298 |
| B | ARG308 |
| B | VAL335 |
| B | ASN339 |
| B | TYR342 |
| B | HOH717 |
| B | HOH744 |
| site_id | BC2 |
| Number of Residues | 29 |
| 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 | HOH650 |
| C | HOH675 |
| C | HOH764 |
| C | HOH766 |
| C | HOH772 |
| C | HOH779 |
| C | HOH807 |
| C | HOH852 |
| D | LYS254 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 502 |
| Chain | Residue |
| C | GTP501 |
| C | HOH764 |
| C | HOH779 |
| C | HOH807 |
| C | HOH959 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 503 |
| Chain | Residue |
| C | ASP39 |
| C | THR41 |
| C | GLY44 |
| C | GLU55 |
| C | HOH780 |
| site_id | BC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE GDP D 600 |
| 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 | MG601 |
| D | MG602 |
| D | HOH705 |
| D | HOH721 |
| D | HOH761 |
| D | HOH795 |
| D | HOH806 |
| D | HOH807 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG D 601 |
| Chain | Residue |
| D | GLN11 |
| D | GDP600 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 602 |
| Chain | Residue |
| D | ASN101 |
| D | GDP600 |
| D | HOH795 |
| D | HOH806 |
| D | HOH807 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 701 |
| Chain | Residue |
| A | HOH817 |
| F | ASP318 |
| F | GLU331 |
| F | ADP703 |
| F | HOH867 |
| site_id | BC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 702 |
| Chain | Residue |
| F | GLU331 |
| F | ASN333 |
| F | ADP703 |
| F | HOH867 |
| site_id | CC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP F 703 |
| Chain | Residue |
| F | LYS74 |
| F | LYS150 |
| F | GLN183 |
| F | LYS184 |
| F | TYR185 |
| F | LEU186 |
| F | LYS198 |
| F | ASP200 |
| F | HIS239 |
| F | LEU240 |
| F | THR241 |
| F | ASN242 |
| F | ILE330 |
| F | GLU331 |
| F | MG701 |
| F | MG702 |
| site_id | CC2 |
| 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 | HIS381 |
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 |
