5ITZ
Crystal structure of the SAC domain of CPAP in a complex with Tubulin and Darpin
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 |
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 | SER178 |
A | GLU183 |
A | ASN206 |
A | TYR224 |
A | ASN228 |
A | GLN11 |
A | ILE231 |
A | MG502 |
A | HOH636 |
A | HOH641 |
A | HOH644 |
A | HOH714 |
A | HOH730 |
A | HOH762 |
A | HOH780 |
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 | HOH636 |
A | HOH641 |
A | HOH644 |
A | HOH780 |
site_id | AC3 |
Number of Residues | 19 |
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 | VAL177 |
B | SER178 |
B | GLU183 |
B | ASN206 |
B | TYR224 |
B | ASN228 |
B | HOH612 |
B | HOH618 |
B | HOH621 |
B | HOH680 |
site_id | AC4 |
Number of Residues | 19 |
Details | binding site for residue LOC B 502 |
Chain | Residue |
A | THR179 |
A | ALA180 |
A | VAL181 |
B | CYS241 |
B | LEU242 |
B | ALA250 |
B | LYS254 |
B | LEU255 |
B | ASN258 |
B | MET259 |
B | THR314 |
B | VAL315 |
B | ALA316 |
B | ILE318 |
B | ASN350 |
B | LYS352 |
B | ILE378 |
B | HOH631 |
B | HOH663 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
D | SER316 | |
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 | THR57 |
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 | SER232 |
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 |