Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7JK5

Structure of Drosophila ORC bound to DNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0000775cellular_componentchromosome, centromeric region
B0000792cellular_componentheterochromatin
B0000808cellular_componentorigin recognition complex
B0003682molecular_functionchromatin binding
B0003688molecular_functionDNA replication origin binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005664cellular_componentnuclear origin of replication recognition complex
B0005694cellular_componentchromosome
B0005723cellular_componentalpha-heterochromatin
B0006260biological_processDNA replication
B0006261biological_processDNA-templated DNA replication
B0006270biological_processDNA replication initiation
B0007052biological_processmitotic spindle organization
B0007076biological_processmitotic chromosome condensation
B0007307biological_processeggshell chorion gene amplification
B0030261biological_processchromosome condensation
C0003677molecular_functionDNA binding
C0003688molecular_functionDNA replication origin binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005643cellular_componentnuclear pore
C0005656cellular_componentnuclear pre-replicative complex
C0005664cellular_componentnuclear origin of replication recognition complex
C0006260biological_processDNA replication
C0006270biological_processDNA replication initiation
C0007611biological_processlearning or memory
C0007612biological_processlearning
C0008355biological_processolfactory learning
C0030536biological_processlarval feeding behavior
C0031261cellular_componentDNA replication preinitiation complex
C0043021molecular_functionribonucleoprotein complex binding
C1903688biological_processpositive regulation of border follicle cell migration
D0000808cellular_componentorigin recognition complex
D0003677molecular_functionDNA binding
D0003688molecular_functionDNA replication origin binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005643cellular_componentnuclear pore
D0005664cellular_componentnuclear origin of replication recognition complex
D0006260biological_processDNA replication
D0006270biological_processDNA replication initiation
D0016887molecular_functionATP hydrolysis activity
D0043021molecular_functionribonucleoprotein complex binding
E0000808cellular_componentorigin recognition complex
E0003688molecular_functionDNA replication origin binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005664cellular_componentnuclear origin of replication recognition complex
E0006260biological_processDNA replication
E0006261biological_processDNA-templated DNA replication
E0006270biological_processDNA replication initiation
E0007052biological_processmitotic spindle organization
E0007076biological_processmitotic chromosome condensation
E0016887molecular_functionATP hydrolysis activity
E0043021molecular_functionribonucleoprotein complex binding
F0000278biological_processmitotic cell cycle
F0000808cellular_componentorigin recognition complex
F0003677molecular_functionDNA binding
F0005096molecular_functionGTPase activator activity
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005664cellular_componentnuclear origin of replication recognition complex
F0005886cellular_componentplasma membrane
F0006260biological_processDNA replication
F0006270biological_processDNA replication initiation
F0032156cellular_componentseptin cytoskeleton
F0032185biological_processseptin cytoskeleton organization
F0042803molecular_functionprotein homodimerization activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q13415
ChainResidueDetails
AVAL564
AGLY598
AASP684
AGLU685
AASN718
AARG784
BTHR170
BTHR181
BTHR258

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:18327897
ChainResidueDetails
ASER533
BSER30
BSER87
BSER91
BSER92
BSER260

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon