4G86
Crystal structure of the redox-active cofactor DBMIB bound to the full length circadian clock protein KaiA from Synechococcus elongatus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007623 | biological_process | circadian rhythm |
| A | 0009649 | biological_process | entrainment of circadian clock |
| A | 0042753 | biological_process | positive regulation of circadian rhythm |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0048511 | biological_process | rhythmic process |
| A | 0051776 | biological_process | detection of redox state |
| B | 0005515 | molecular_function | protein binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007623 | biological_process | circadian rhythm |
| B | 0009649 | biological_process | entrainment of circadian clock |
| B | 0042753 | biological_process | positive regulation of circadian rhythm |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0048511 | biological_process | rhythmic process |
| B | 0051776 | biological_process | detection of redox state |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BNT A 301 |
| Chain | Residue |
| A | SER62 |
| A | PHE63 |
| A | ARG64 |
| A | ALA65 |
| A | ARG85 |
| A | SER87 |
| B | LYS246 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PE A 302 |
| Chain | Residue |
| A | ALA23 |
| A | GLU112 |
| A | PRO115 |
| A | 2PE303 |
| A | HOH401 |
| A | HOH416 |
| B | BNT1301 |
| A | ASP19 |
| A | ARG22 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 2PE A 303 |
| Chain | Residue |
| A | ARG22 |
| A | 1PE302 |
| A | HOH472 |
| B | TYR185 |
| B | BNT1301 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BNT A 304 |
| Chain | Residue |
| A | ARG180 |
| A | PRO229 |
| A | THR231 |
| B | GLU274 |
| B | ARG277 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BNT B 1301 |
| Chain | Residue |
| A | GLU112 |
| A | TYR116 |
| A | 1PE302 |
| A | 2PE303 |
| B | LEU182 |
| B | GLU186 |
| B | LYS189 |
| B | LEU190 |
| B | ALA193 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BNT B 1302 |
| Chain | Residue |
| B | ALA58 |
| B | ALA59 |
| B | ASN60 |
| B | PRO61 |
| B | SER62 |
| B | PHE63 |
| B | ARG64 |
| B | ALA65 |
| B | ARG85 |
| B | ASP86 |
| B | HOH1444 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1303 |
| Chain | Residue |
| A | LEU104 |
| A | HOH493 |
| B | ASN221 |
| B | MET275 |
| B | ARG278 |
| B | HOH1453 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1304 |
| Chain | Residue |
| A | GLU124 |
| A | HOH493 |
| B | MET275 |
| B | ARG278 |
| B | SER279 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 326 |
| Details | Domain: {"description":"KaiA N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00760","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15007067","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 216 |
| Details | Domain: {"description":"KaiA C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00761","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15007067","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 268 |
| Details | Region: {"description":"PsR domain, binds oxidized quinones","evidences":[{"source":"PubMed","id":"20231482","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Region: {"description":"Flexible linker","evidences":[{"source":"PubMed","id":"15007067","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
