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1QHH

STRUCTURE OF DNA HELICASE WITH ADPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003678molecular_functionDNA helicase activity
A0005524molecular_functionATP binding
B0003677molecular_functionDNA binding
B0003678molecular_functionDNA helicase activity
B0005524molecular_functionATP binding
B0016787molecular_functionhydrolase activity
D0003677molecular_functionDNA binding
D0003678molecular_functionDNA helicase activity
D0005524molecular_functionATP binding
D0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP A 700
ChainResidue
AHIS11
BGLN254
BTYR286
BARG287
BHOH791
DGLY569
DGLU571
DARG610
ALEU12
AASN13
AGLN16
AALA33
AGLY34
AGLY36
ATHR38
AARG39

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00560","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10388562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10388562","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 833
ChainResidueDetails
DARG610electrostatic stabiliser
BGLU224proton acceptor
BGLN254electrostatic stabiliser

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PDB entries from 2025-07-16

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