2Z4R
Crystal structure of domain III from the Thermotoga maritima replication initiation protein DnaA
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003688 | molecular_function | DNA replication origin binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006260 | biological_process | DNA replication |
| A | 0006270 | biological_process | DNA replication initiation |
| A | 0006275 | biological_process | regulation of DNA replication |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0043565 | molecular_function | sequence-specific DNA binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003688 | molecular_function | DNA replication origin binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006260 | biological_process | DNA replication |
| B | 0006270 | biological_process | DNA replication initiation |
| B | 0006275 | biological_process | regulation of DNA replication |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0043565 | molecular_function | sequence-specific DNA binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003688 | molecular_function | DNA replication origin binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006260 | biological_process | DNA replication |
| C | 0006270 | biological_process | DNA replication initiation |
| C | 0006275 | biological_process | regulation of DNA replication |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0043565 | molecular_function | sequence-specific DNA binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 500 |
| Chain | Residue |
| A | THR144 |
| A | ASP201 |
| A | ASP202 |
| A | ADP501 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 501 |
| Chain | Residue |
| B | THR144 |
| B | ASP201 |
| B | ASP202 |
| B | ADP502 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 502 |
| Chain | Residue |
| C | ASP201 |
| C | ASP202 |
| C | ADP503 |
| C | THR144 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP A 501 |
| Chain | Residue |
| A | TYR102 |
| A | ASN106 |
| A | PHE107 |
| A | VAL108 |
| A | ASN113 |
| A | GLY138 |
| A | VAL139 |
| A | GLY140 |
| A | LEU141 |
| A | GLY142 |
| A | LYS143 |
| A | THR144 |
| A | HIS145 |
| A | ILE271 |
| A | LEU299 |
| A | ARG300 |
| A | MG500 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP B 502 |
| Chain | Residue |
| B | TYR102 |
| B | ASN106 |
| B | PHE107 |
| B | VAL108 |
| B | ASN113 |
| B | GLY138 |
| B | VAL139 |
| B | GLY140 |
| B | LEU141 |
| B | GLY142 |
| B | LYS143 |
| B | THR144 |
| B | HIS145 |
| B | ILE271 |
| B | LEU299 |
| B | ARG300 |
| B | MG501 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP C 503 |
| Chain | Residue |
| C | TYR102 |
| C | ASN106 |
| C | PHE107 |
| C | VAL108 |
| C | ASN113 |
| C | GLY138 |
| C | VAL139 |
| C | GLY140 |
| C | LEU141 |
| C | GLY142 |
| C | LYS143 |
| C | THR144 |
| C | HIS145 |
| C | ILE271 |
| C | LEU299 |
| C | ARG300 |
| C | MG502 |
Functional Information from PROSITE/UniProt
| site_id | PS01008 |
| Number of Residues | 19 |
| Details | DNAA DnaA protein signature. IAekFN.RsHPVVvdSvkkV |
| Chain | Residue | Details |
| A | ILE393-VAL411 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255 |
| Chain | Residue | Details |
| A | GLY137 | |
| B | GLY137 | |
| C | GLY137 |
