3K0E
Crystal structure of the phosphorylation-site mutant T426N of the KaiC circadian clock protein
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 | 0009649 | biological_process | entrainment of circadian clock |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0042752 | biological_process | regulation of circadian rhythm |
| A | 0042754 | biological_process | negative regulation of circadian rhythm |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048511 | biological_process | rhythmic process |
| A | 0070297 | biological_process | regulation of phosphorelay signal transduction system |
| 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 | 0009649 | biological_process | entrainment of circadian clock |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0042752 | biological_process | regulation of circadian rhythm |
| B | 0042754 | biological_process | negative regulation of circadian rhythm |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048511 | biological_process | rhythmic process |
| B | 0070297 | biological_process | regulation of phosphorelay signal transduction system |
| 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 | 0009649 | biological_process | entrainment of circadian clock |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0042752 | biological_process | regulation of circadian rhythm |
| C | 0042754 | biological_process | negative regulation of circadian rhythm |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0048511 | biological_process | rhythmic process |
| C | 0070297 | biological_process | regulation of phosphorelay signal transduction system |
| C | 0106310 | molecular_function | protein serine kinase activity |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0007623 | biological_process | circadian rhythm |
| D | 0009649 | biological_process | entrainment of circadian clock |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0042752 | biological_process | regulation of circadian rhythm |
| D | 0042754 | biological_process | negative regulation of circadian rhythm |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0048511 | biological_process | rhythmic process |
| D | 0070297 | biological_process | regulation of phosphorelay signal transduction system |
| D | 0106310 | molecular_function | protein serine kinase activity |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003677 | molecular_function | DNA binding |
| E | 0004674 | molecular_function | protein serine/threonine kinase activity |
| E | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0007623 | biological_process | circadian rhythm |
| E | 0009649 | biological_process | entrainment of circadian clock |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0042752 | biological_process | regulation of circadian rhythm |
| E | 0042754 | biological_process | negative regulation of circadian rhythm |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0048511 | biological_process | rhythmic process |
| E | 0070297 | biological_process | regulation of phosphorelay signal transduction system |
| E | 0106310 | molecular_function | protein serine kinase activity |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0003677 | molecular_function | DNA binding |
| F | 0004674 | molecular_function | protein serine/threonine kinase activity |
| F | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0007623 | biological_process | circadian rhythm |
| F | 0009649 | biological_process | entrainment of circadian clock |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0042752 | biological_process | regulation of circadian rhythm |
| F | 0042754 | biological_process | negative regulation of circadian rhythm |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0048511 | biological_process | rhythmic process |
| F | 0070297 | biological_process | regulation of phosphorelay signal transduction system |
| F | 0106310 | molecular_function | protein serine kinase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 801 |
| Chain | Residue |
| A | THR295 |
| A | GLU318 |
| A | GLU319 |
| A | ASP378 |
| A | MG802 |
| A | ATP901 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 802 |
| Chain | Residue |
| A | MG801 |
| A | ATP901 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 701 |
| Chain | Residue |
| A | GLU77 |
| A | ATP903 |
| A | THR53 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP A 901 |
| Chain | Residue |
| A | THR290 |
| A | GLY291 |
| A | THR292 |
| A | GLY293 |
| A | LYS294 |
| A | THR295 |
| A | LEU296 |
| A | GLU318 |
| A | GLU319 |
| A | TRP331 |
| A | ARG451 |
| A | ILE472 |
| A | SER473 |
| A | MG801 |
| A | MG802 |
| B | LYS457 |
| B | MET458 |
| B | ARG459 |
| B | GLY460 |
| B | SER461 |
| B | TRP462 |
| B | HIS463 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ATP A 903 |
| Chain | Residue |
| A | GLY49 |
| A | THR50 |
| A | GLY51 |
| A | LYS52 |
| A | THR53 |
| A | LEU54 |
| A | GLU77 |
| A | GLU78 |
| A | SER89 |
| A | PHE90 |
| A | ARG218 |
| A | ILE239 |
| A | THR240 |
| A | ASP241 |
| A | HOH526 |
| A | MG701 |
| B | LEU223 |
| B | LYS224 |
| B | LEU225 |
| B | ARG226 |
| B | THR228 |
| B | SER229 |
| B | HIS230 |
| B | LYS232 |
| B | MG702 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 702 |
| Chain | Residue |
| A | LYS224 |
| F | SER48 |
| F | ATP903 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 702 |
| Chain | Residue |
| A | SER48 |
| A | ATP903 |
| B | PHE199 |
| B | LYS224 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 802 |
| Chain | Residue |
| B | GLU318 |
| B | HOH522 |
| B | MG801 |
| B | ATP901 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 801 |
| Chain | Residue |
| B | THR295 |
| B | GLU318 |
| B | GLU319 |
| B | HOH522 |
| B | MG802 |
| B | ATP901 |
| C | ARG459 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 701 |
| Chain | Residue |
| B | THR53 |
| B | ASP145 |
| B | ATP903 |
| site_id | BC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP B 901 |
| Chain | Residue |
| B | THR290 |
| B | GLY291 |
| B | THR292 |
| B | GLY293 |
| B | LYS294 |
| B | THR295 |
| B | TRP331 |
| B | ARG451 |
| B | ILE472 |
| B | ASP474 |
| B | HOH522 |
| B | MG801 |
| B | MG802 |
| C | LYS457 |
| C | MET458 |
| C | ARG459 |
| C | SER461 |
| C | TRP462 |
| C | HIS463 |
| site_id | BC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP B 903 |
| Chain | Residue |
| B | THR50 |
| B | GLY51 |
| B | LYS52 |
| B | THR53 |
| B | LEU54 |
| B | GLU78 |
| B | SER89 |
| B | PHE90 |
| B | ILE239 |
| B | THR240 |
| B | MG701 |
| C | LYS224 |
| C | LEU225 |
| C | ARG226 |
| C | THR228 |
| C | SER229 |
| C | HIS230 |
| C | LYS232 |
| B | GLY49 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 801 |
| Chain | Residue |
| C | THR295 |
| C | GLU318 |
| C | MG802 |
| C | ATP901 |
| D | ARG459 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 802 |
| Chain | Residue |
| C | THR290 |
| C | MG801 |
| C | ATP901 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 702 |
| Chain | Residue |
| C | THR53 |
| C | GLU78 |
| C | ATP903 |
| D | ARG226 |
| site_id | BC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP C 901 |
| Chain | Residue |
| C | THR290 |
| C | GLY291 |
| C | THR292 |
| C | GLY293 |
| C | LYS294 |
| C | THR295 |
| C | SER330 |
| C | TRP331 |
| C | ARG451 |
| C | ILE472 |
| C | MG801 |
| C | MG802 |
| D | LYS457 |
| D | MET458 |
| D | ARG459 |
| D | SER461 |
| D | HIS463 |
| D | LYS465 |
| site_id | BC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP C 903 |
| Chain | Residue |
| C | SER48 |
| C | GLY49 |
| C | THR50 |
| C | GLY51 |
| C | LYS52 |
| C | THR53 |
| C | LEU54 |
| C | SER89 |
| C | PHE90 |
| C | ILE239 |
| C | THR240 |
| C | ASP241 |
| C | MG701 |
| C | MG702 |
| D | PHE199 |
| D | LYS224 |
| D | LEU225 |
| D | THR228 |
| D | HIS230 |
| D | LYS232 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 701 |
| Chain | Residue |
| C | THR53 |
| C | ASP145 |
| C | ATP903 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 802 |
| Chain | Residue |
| D | THR295 |
| D | GLU319 |
| D | MG801 |
| D | ATP901 |
| E | ARG459 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 801 |
| Chain | Residue |
| D | LYS294 |
| D | MG802 |
| D | ATP901 |
| site_id | CC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 520 |
| Chain | Residue |
| D | THR53 |
| D | GLU78 |
| D | ATP903 |
| site_id | CC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ATP D 901 |
| Chain | Residue |
| D | THR290 |
| D | GLY291 |
| D | THR292 |
| D | GLY293 |
| D | LYS294 |
| D | THR295 |
| D | LEU296 |
| D | GLU318 |
| D | TRP331 |
| D | ARG451 |
| D | ILE472 |
| D | SER473 |
| D | HOH537 |
| D | MG801 |
| D | MG802 |
| E | LYS457 |
| E | MET458 |
| E | ARG459 |
| E | GLY460 |
| E | SER461 |
| E | HIS463 |
| site_id | CC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP D 903 |
| Chain | Residue |
| D | SER48 |
| D | GLY49 |
| D | THR50 |
| D | GLY51 |
| D | LYS52 |
| D | THR53 |
| D | LEU54 |
| D | SER89 |
| D | PHE90 |
| D | ILE239 |
| D | ASP241 |
| D | MG520 |
| E | LYS224 |
| E | ARG226 |
| E | GLY227 |
| E | THR228 |
| E | HIS230 |
| E | LYS232 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG E 801 |
| Chain | Residue |
| E | THR295 |
| E | GLU318 |
| E | ATP901 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 702 |
| Chain | Residue |
| E | LYS52 |
| E | THR53 |
| E | ASP145 |
| E | THR181 |
| E | ATP903 |
| site_id | CC8 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP E 901 |
| Chain | Residue |
| E | THR290 |
| E | GLY291 |
| E | THR292 |
| E | GLY293 |
| E | LYS294 |
| E | THR295 |
| E | LEU296 |
| E | SER330 |
| E | TRP331 |
| E | ARG451 |
| E | ILE472 |
| E | SER473 |
| E | ASP474 |
| E | MG801 |
| F | LYS457 |
| F | MET458 |
| F | ARG459 |
| F | SER461 |
| F | TRP462 |
| F | HIS463 |
| site_id | CC9 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ATP E 903 |
| Chain | Residue |
| E | GLY49 |
| E | THR50 |
| E | GLY51 |
| E | LYS52 |
| E | THR53 |
| E | LEU54 |
| E | GLU78 |
| E | SER89 |
| E | PHE90 |
| E | ILE239 |
| E | THR240 |
| E | HOH522 |
| E | MG702 |
| F | LEU223 |
| F | LYS224 |
| F | ARG226 |
| F | THR228 |
| F | SER229 |
| F | HIS230 |
| F | MG701 |
| site_id | DC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 802 |
| Chain | Residue |
| F | THR295 |
| F | GLU318 |
| F | GLU319 |
| F | ATP901 |
| site_id | DC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG F 701 |
| Chain | Residue |
| E | SER48 |
| E | ATP903 |
| F | LYS224 |
| site_id | DC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 520 |
| Chain | Residue |
| F | LYS52 |
| F | THR53 |
| F | ASP145 |
| F | ATP903 |
| site_id | DC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP F 901 |
| Chain | Residue |
| A | TPO432 |
| A | LYS457 |
| A | MET458 |
| A | ARG459 |
| A | GLY460 |
| A | SER461 |
| A | TRP462 |
| A | HIS463 |
| A | LYS465 |
| F | GLY291 |
| F | THR292 |
| F | GLY293 |
| F | LYS294 |
| F | THR295 |
| F | LEU296 |
| F | GLU318 |
| F | SER330 |
| F | TRP331 |
| F | ARG451 |
| F | ILE472 |
| F | SER473 |
| F | MG802 |
| site_id | DC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP F 903 |
| Chain | Residue |
| A | LYS224 |
| A | LEU225 |
| A | ARG226 |
| A | THR228 |
| A | HIS230 |
| A | MG702 |
| F | GLY49 |
| F | THR50 |
| F | GLY51 |
| F | LYS52 |
| F | THR53 |
| F | LEU54 |
| F | GLU78 |
| F | SER89 |
| F | PHE90 |
| F | ILE239 |
| F | THR240 |
| F | ASP241 |
| F | MG520 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor in CI (KaiC 1) => ECO:0000305|PubMed:22304631 |
| Chain | Residue | Details |
| A | GLU77 | |
| B | GLU77 | |
| C | GLU77 | |
| D | GLU77 | |
| E | GLU77 | |
| F | GLU77 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor in CII (KaiC 2) => ECO:0000305|PubMed:22304631 |
| Chain | Residue | Details |
| A | GLU318 | |
| B | GLU318 | |
| C | GLU318 | |
| D | GLU318 | |
| E | GLU318 | |
| F | GLU318 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 150 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:16628225, ECO:0000269|PubMed:22304631, ECO:0007744|PDB:1TF7, ECO:0007744|PDB:2GBL, ECO:0007744|PDB:4DUG |
| Chain | Residue | Details |
| A | GLY49 | |
| A | HIS230 | |
| D | LYS465 | |
| E | GLY49 | |
| E | THR50 | |
| E | GLY51 | |
| E | LYS52 | |
| E | LEU54 | |
| E | SER89 | |
| E | LYS224 | |
| E | ARG226 | |
| E | THR228 | |
| A | THR240 | |
| E | HIS230 | |
| E | THR240 | |
| E | ASP241 | |
| E | THR290 | |
| E | GLY291 | |
| E | THR292 | |
| E | GLY293 | |
| E | LYS294 | |
| E | LEU296 | |
| E | TRP331 | |
| A | ASP241 | |
| E | ARG451 | |
| E | LYS457 | |
| E | ARG459 | |
| E | SER461 | |
| E | HIS463 | |
| E | LYS465 | |
| F | GLY49 | |
| F | THR50 | |
| F | GLY51 | |
| F | LYS52 | |
| A | THR290 | |
| F | LEU54 | |
| F | SER89 | |
| F | LYS224 | |
| F | ARG226 | |
| F | THR228 | |
| F | HIS230 | |
| F | THR240 | |
| F | ASP241 | |
| F | THR290 | |
| F | GLY291 | |
| A | GLY291 | |
| F | THR292 | |
| F | GLY293 | |
| F | LYS294 | |
| F | LEU296 | |
| F | TRP331 | |
| F | ARG451 | |
| F | LYS457 | |
| F | ARG459 | |
| F | SER461 | |
| F | HIS463 | |
| A | THR292 | |
| F | LYS465 | |
| A | GLY293 | |
| A | LYS294 | |
| A | LEU296 | |
| A | TRP331 | |
| A | THR50 | |
| A | ARG451 | |
| A | LYS457 | |
| A | ARG459 | |
| A | SER461 | |
| A | HIS463 | |
| A | LYS465 | |
| B | GLY49 | |
| B | THR50 | |
| B | GLY51 | |
| B | LYS52 | |
| A | GLY51 | |
| B | LEU54 | |
| B | SER89 | |
| B | LYS224 | |
| B | ARG226 | |
| B | THR228 | |
| B | HIS230 | |
| B | THR240 | |
| B | ASP241 | |
| B | THR290 | |
| B | GLY291 | |
| A | LYS52 | |
| B | THR292 | |
| B | GLY293 | |
| B | LYS294 | |
| B | LEU296 | |
| B | TRP331 | |
| B | ARG451 | |
| B | LYS457 | |
| B | ARG459 | |
| B | SER461 | |
| B | HIS463 | |
| A | LEU54 | |
| B | LYS465 | |
| C | GLY49 | |
| C | THR50 | |
| C | GLY51 | |
| C | LYS52 | |
| C | LEU54 | |
| C | SER89 | |
| C | LYS224 | |
| C | ARG226 | |
| C | THR228 | |
| A | SER89 | |
| C | HIS230 | |
| C | THR240 | |
| C | ASP241 | |
| C | THR290 | |
| C | GLY291 | |
| C | THR292 | |
| C | GLY293 | |
| C | LYS294 | |
| C | LEU296 | |
| C | TRP331 | |
| A | LYS224 | |
| C | ARG451 | |
| C | LYS457 | |
| C | ARG459 | |
| C | SER461 | |
| C | HIS463 | |
| C | LYS465 | |
| D | GLY49 | |
| D | THR50 | |
| D | GLY51 | |
| D | LYS52 | |
| A | ARG226 | |
| D | LEU54 | |
| D | SER89 | |
| D | LYS224 | |
| D | ARG226 | |
| D | THR228 | |
| D | HIS230 | |
| D | THR240 | |
| D | ASP241 | |
| D | THR290 | |
| D | GLY291 | |
| A | THR228 | |
| D | THR292 | |
| D | GLY293 | |
| D | LYS294 | |
| D | LEU296 | |
| D | TRP331 | |
| D | ARG451 | |
| D | LYS457 | |
| D | ARG459 | |
| D | SER461 | |
| D | HIS463 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0007744|PDB:4DUG, ECO:0007744|PDB:4TL6, ECO:0007744|PDB:7DXQ |
| Chain | Residue | Details |
| A | THR53 | |
| B | THR53 | |
| C | THR53 | |
| D | THR53 | |
| E | THR53 | |
| F | THR53 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:16628225, ECO:0007744|PDB:1TF7, ECO:0007744|PDB:2GBL |
| Chain | Residue | Details |
| A | LEU225 | |
| E | MET458 | |
| F | LEU225 | |
| F | MET458 | |
| A | MET458 | |
| B | LEU225 | |
| B | MET458 | |
| C | LEU225 | |
| C | MET458 | |
| D | LEU225 | |
| D | MET458 | |
| E | LEU225 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:16628225, ECO:0007744|PDB:1U9I, ECO:0007744|PDB:2GBL, ECO:0007744|PDB:4DUG, ECO:0007744|PDB:7DXQ |
| Chain | Residue | Details |
| A | THR295 | |
| B | THR295 | |
| C | THR295 | |
| D | THR295 | |
| E | THR295 | |
| F | THR295 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:16628225 |
| Chain | Residue | Details |
| A | GLU318 | |
| B | GLU318 | |
| C | GLU318 | |
| D | GLU318 | |
| E | GLU318 | |
| F | GLU318 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15347809, ECO:0000269|PubMed:15347812, ECO:0000269|PubMed:17717528, ECO:0000269|PubMed:17916691, ECO:0007744|PDB:1U9I, ECO:0007744|PDB:2GBL |
| Chain | Residue | Details |
| A | SEP431 | |
| B | SEP431 | |
| C | SEP431 | |
| D | SEP431 | |
| E | SEP431 | |
| F | SEP431 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000255|HAMAP-Rule:MF_01836, ECO:0000269|PubMed:15304218, ECO:0000269|PubMed:15347809, ECO:0000269|PubMed:15347812, ECO:0000269|PubMed:17717528, ECO:0000269|PubMed:17916691, ECO:0007744|PDB:1U9I, ECO:0007744|PDB:2GBL |
| Chain | Residue | Details |
| A | TPO432 | |
| B | TPO432 | |
| C | TPO432 | |
| D | TPO432 | |
| E | TPO432 | |
| F | TPO432 |
