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3PJR

HELICASE SUBSTRATE COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0000725biological_processrecombinational repair
A0003677molecular_functionDNA binding
A0003678molecular_functionDNA helicase activity
A0004386molecular_functionhelicase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006268biological_processDNA unwinding involved in DNA replication
A0016787molecular_functionhydrolase activity
A0016853molecular_functionisomerase activity
A0016887molecular_functionATP hydrolysis activity
A0033202cellular_componentDNA helicase complex
A0043138molecular_function3'-5' DNA helicase activity
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ATP A 725
ChainResidue
AHIS11
AGLN254
ATYR286
AARG287
AGLU571
AARG610
ALEU12
AGLN16
AALA33
ASER35
AGLY36
ALYS37
ATHR38
AARG39

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00560, ECO:0000269|PubMed:10388562
ChainResidueDetails
AHIS11
AGLY34

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10388562
ChainResidueDetails
AARG287

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qhg
ChainResidueDetails
AGLU224
ALYS37
AARG610

site_idMCSA1
Number of Residues6
DetailsM-CSA 833
ChainResidueDetails
ALYS37electrostatic stabiliser
ATHR38metal ligand
AASP223electrostatic stabiliser
AGLU224proton acceptor
AGLN254electrostatic stabiliser
AARG610electrostatic stabiliser

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PDB entries from 2024-07-24

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