4O0M
Crystal structure of T. Elongatus BP-1 Clock Protein KaiC
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0007623 | biological_process | circadian rhythm |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0042752 | biological_process | regulation of circadian rhythm |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046777 | biological_process | protein autophosphorylation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048511 | biological_process | rhythmic process |
| A | 0106310 | molecular_function | protein serine kinase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0007623 | biological_process | circadian rhythm |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0042752 | biological_process | regulation of circadian rhythm |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046777 | biological_process | protein autophosphorylation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048511 | biological_process | rhythmic process |
| B | 0106310 | molecular_function | protein serine kinase activity |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0007623 | biological_process | circadian rhythm |
| C | 0016301 | molecular_function | kinase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0042752 | biological_process | regulation of circadian rhythm |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046777 | biological_process | protein autophosphorylation |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048511 | biological_process | rhythmic process |
| C | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 801 |
| Chain | Residue |
| A | THR295 |
| A | GLU319 |
| A | ATP802 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP A 802 |
| Chain | Residue |
| A | LEU296 |
| A | GLU318 |
| A | TRP331 |
| A | ARG451 |
| A | ILE472 |
| A | MG801 |
| B | LYS457 |
| B | MET458 |
| B | ARG459 |
| B | SER461 |
| B | TRP462 |
| B | HIS463 |
| A | THR290 |
| A | GLY291 |
| A | THR292 |
| A | GLY293 |
| A | LYS294 |
| A | THR295 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP A 803 |
| Chain | Residue |
| A | GLY50 |
| A | THR51 |
| A | GLY52 |
| A | LYS53 |
| A | THR54 |
| A | LEU55 |
| A | SER90 |
| A | PHE91 |
| A | ILE240 |
| A | MG804 |
| B | LYS225 |
| B | LEU226 |
| B | ARG227 |
| B | THR229 |
| B | THR230 |
| B | HIS231 |
| B | LYS233 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 804 |
| Chain | Residue |
| A | THR54 |
| A | GLU79 |
| A | ASP146 |
| A | ATP803 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 601 |
| Chain | Residue |
| B | THR295 |
| B | GLU318 |
| B | GLU319 |
| B | ATP602 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP B 602 |
| Chain | Residue |
| B | THR290 |
| B | GLY291 |
| B | THR292 |
| B | GLY293 |
| B | LYS294 |
| B | THR295 |
| B | LEU296 |
| B | GLU318 |
| B | TRP331 |
| B | THR415 |
| B | ARG451 |
| B | ILE472 |
| B | MG601 |
| C | LYS457 |
| C | MET458 |
| C | ARG459 |
| C | SER461 |
| C | TRP462 |
| C | HIS463 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 603 |
| Chain | Residue |
| B | THR54 |
| B | GLU79 |
| B | ATP604 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP B 604 |
| Chain | Residue |
| B | SER49 |
| B | GLY50 |
| B | THR51 |
| B | GLY52 |
| B | LYS53 |
| B | THR54 |
| B | LEU55 |
| B | SER90 |
| B | PHE91 |
| B | ARG219 |
| B | ILE240 |
| B | MG603 |
| C | PHE200 |
| C | LYS225 |
| C | LEU226 |
| C | ARG227 |
| C | THR229 |
| C | THR230 |
| C | HIS231 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG C 601 |
| Chain | Residue |
| C | THR295 |
| C | ATP602 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP C 602 |
| Chain | Residue |
| C | THR295 |
| C | LEU296 |
| C | TRP331 |
| C | THR415 |
| C | ARG451 |
| C | ILE472 |
| C | MG601 |
| C | HOH704 |
| A | LYS457 |
| A | MET458 |
| A | ARG459 |
| A | SER461 |
| A | HIS463 |
| C | THR290 |
| C | GLY291 |
| C | THR292 |
| C | GLY293 |
| C | LYS294 |
| site_id | BC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP C 603 |
| Chain | Residue |
| A | PHE200 |
| A | LYS225 |
| A | ARG227 |
| A | THR229 |
| A | THR230 |
| A | HIS231 |
| A | HOH950 |
| C | SER49 |
| C | GLY50 |
| C | THR51 |
| C | GLY52 |
| C | LYS53 |
| C | THR54 |
| C | LEU55 |
| C | SER90 |
| C | PHE91 |
| C | ARG219 |
| C | ILE240 |
| C | MG604 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 604 |
| Chain | Residue |
| C | THR54 |
| C | ASP146 |
| C | ATP603 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor in CI (KaiC 1) => ECO:0000305|PubMed:35507871 |
| Chain | Residue | Details |
| A | GLU78 | |
| B | GLU78 | |
| C | GLU78 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor in CII (KaiC 2) => ECO:0000305|PubMed:35507871 |
| Chain | Residue | Details |
| A | GLU318 | |
| B | GLU318 | |
| C | GLU318 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000312|PDB:7DY1 |
| Chain | Residue | Details |
| A | SER49 | |
| B | SER49 | |
| C | SER49 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 63 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000312|PDB:7DY1 |
| Chain | Residue | Details |
| A | GLY50 | |
| A | HIS231 | |
| A | THR290 | |
| A | GLY291 | |
| A | THR292 | |
| A | GLY293 | |
| A | LYS294 | |
| A | THR295 | |
| A | LEU296 | |
| A | ARG451 | |
| A | LYS457 | |
| A | THR51 | |
| A | MET458 | |
| A | ARG459 | |
| B | GLY50 | |
| B | THR51 | |
| B | GLY52 | |
| B | LYS53 | |
| B | LEU55 | |
| B | SER90 | |
| B | LYS225 | |
| B | LEU226 | |
| A | GLY52 | |
| B | ARG227 | |
| B | HIS231 | |
| B | THR290 | |
| B | GLY291 | |
| B | THR292 | |
| B | GLY293 | |
| B | LYS294 | |
| B | THR295 | |
| B | LEU296 | |
| B | ARG451 | |
| A | LYS53 | |
| B | LYS457 | |
| B | MET458 | |
| B | ARG459 | |
| C | GLY50 | |
| C | THR51 | |
| C | GLY52 | |
| C | LYS53 | |
| C | LEU55 | |
| C | SER90 | |
| C | LYS225 | |
| A | LEU55 | |
| C | LEU226 | |
| C | ARG227 | |
| C | HIS231 | |
| C | THR290 | |
| C | GLY291 | |
| C | THR292 | |
| C | GLY293 | |
| C | LYS294 | |
| C | THR295 | |
| C | LEU296 | |
| A | SER90 | |
| C | ARG451 | |
| C | LYS457 | |
| C | MET458 | |
| C | ARG459 | |
| A | LYS225 | |
| A | LEU226 | |
| A | ARG227 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 21 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836 |
| Chain | Residue | Details |
| A | THR54 | |
| B | GLU318 | |
| B | TRP331 | |
| B | SER461 | |
| B | HIS463 | |
| B | LYS465 | |
| C | THR54 | |
| C | THR229 | |
| C | GLU318 | |
| C | TRP331 | |
| C | SER461 | |
| A | THR229 | |
| C | HIS463 | |
| C | LYS465 | |
| A | GLU318 | |
| A | TRP331 | |
| A | SER461 | |
| A | HIS463 | |
| A | LYS465 | |
| B | THR54 | |
| B | THR229 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:24112939 |
| Chain | Residue | Details |
| A | SEP431 | |
| B | SEP431 | |
| C | SEP431 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:24112939 |
| Chain | Residue | Details |
| A | TPO432 | |
| B | TPO432 | |
| C | TPO432 |
