Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003677 | molecular_function | DNA binding |
A | 0003678 | molecular_function | DNA helicase activity |
A | 0004386 | molecular_function | helicase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005829 | cellular_component | cytosol |
A | 0006260 | biological_process | DNA replication |
A | 0006269 | biological_process | DNA replication, synthesis of primer |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0042802 | molecular_function | identical protein binding |
A | 1990077 | cellular_component | primosome complex |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003677 | molecular_function | DNA binding |
B | 0003678 | molecular_function | DNA helicase activity |
B | 0004386 | molecular_function | helicase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005829 | cellular_component | cytosol |
B | 0006260 | biological_process | DNA replication |
B | 0006269 | biological_process | DNA replication, synthesis of primer |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0042802 | molecular_function | identical protein binding |
B | 1990077 | cellular_component | primosome complex |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 500 |
Chain | Residue |
A | ARG211 |
A | SER213 |
A | VAL214 |
A | GLY215 |
A | LYS216 |
A | THR217 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 500 |
Chain | Residue |
B | GLY215 |
B | LYS216 |
B | THR217 |
B | ARG211 |
B | SER213 |
B | VAL214 |
Functional Information from PROSITE/UniProt
site_id | PS00039 |
Number of Residues | 9 |
Details | DEAD_ATP_HELICASE DEAD-box subfamily ATP-dependent helicases signature. LLDEADRkI |
Chain | Residue | Details |
A | LEU139-ILE147 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"12235389","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23022319","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23022319","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4ESV","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23022319","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"23022319","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ESV","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Site: {"description":"Gamma-phosphate sensor","evidences":[{"source":"PubMed","id":"12235389","evidenceCode":"ECO:0000305"}]} |