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5UJM

Structure of the active form of human Origin Recognition Complex and its ATPase motor module

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0016887molecular_functionATP hydrolysis activity
B0000808cellular_componentorigin recognition complex
B0005634cellular_componentnucleus
B0006260biological_processDNA replication
C0003677molecular_functionDNA binding
C0005664cellular_componentnuclear origin of replication recognition complex
C0006260biological_processDNA replication
D0000166molecular_functionnucleotide binding
D0000781cellular_componentchromosome, telomeric region
D0000808cellular_componentorigin recognition complex
D0003677molecular_functionDNA binding
D0003688molecular_functionDNA replication origin binding
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005664cellular_componentnuclear origin of replication recognition complex
D0005730cellular_componentnucleolus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006260biological_processDNA replication
D0006270biological_processDNA replication initiation
D0016887molecular_functionATP hydrolysis activity
D0040038biological_processpolar body extrusion after meiotic divisions
D0051258biological_processprotein polymerization
E0000166molecular_functionnucleotide binding
E0000781cellular_componentchromosome, telomeric region
E0000785cellular_componentchromatin
E0000808cellular_componentorigin recognition complex
E0003674molecular_functionmolecular_function
E0003688molecular_functionDNA replication origin binding
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005664cellular_componentnuclear origin of replication recognition complex
E0005694cellular_componentchromosome
E0005829cellular_componentcytosol
E0006260biological_processDNA replication
E0006270biological_processDNA replication initiation
E0006275biological_processregulation of DNA replication
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue ATP A 901
ChainResidue
AVAL500
AASN654
ATYR681
AILE689
AALA719
AARG720
ALEU723
AMG902
DARG209
AGLU502
ACYS506
APRO536
AGLY539
ALYS540
ATHR541
AALA542
AGLU621

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 902
ChainResidue
ATHR541
AASP620
AGLU621
AATP901

site_idAC3
Number of Residues17
Detailsbinding site for residue ATP D 901
ChainResidue
DGLN31
DASN36
DPHE38
DVAL40
DPRO68
DARG69
DGLY70
DSER71
DGLY72
DLYS73
DTHR74
DMET75
DLEU276
DARG277
DHIS280
DMG902
EARG143

site_idAC4
Number of Residues4
Detailsbinding site for residue MG D 902
ChainResidue
DTHR74
DASP159
DATP901
EARG143

site_idAC5
Number of Residues15
Detailsbinding site for residue ATP E 501
ChainResidue
ELEU9
EHIS38
ETHR39
EALA40
ESER41
EGLY42
ELYS43
ETHR44
ETYR45
EASP125
EGLU159
ETYR182
EILE190
ELEU222
EARG226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
EGLY37
AASN654
AARG720

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-methyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
DLYS7
AASP620
AGLU621

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER478

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PDB entries from 2024-07-24

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