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1NED

CRYSTAL STRUCTURE OF HSLV (CLPQ) AT 3.8 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003824molecular_functioncatalytic activity
A0004176molecular_functionATP-dependent peptidase activity
A0004298molecular_functionthreonine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005839cellular_componentproteasome core complex
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0009376cellular_componentHslUV protease complex
A0009408biological_processresponse to heat
A0016787molecular_functionhydrolase activity
A0019904molecular_functionprotein domain specific binding
A0030163biological_processprotein catabolic process
A0030164biological_processprotein denaturation
A0034605biological_processcellular response to heat
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0051603biological_processproteolysis involved in protein catabolic process
B0000287molecular_functionmagnesium ion binding
B0003824molecular_functioncatalytic activity
B0004176molecular_functionATP-dependent peptidase activity
B0004298molecular_functionthreonine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005839cellular_componentproteasome core complex
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0009376cellular_componentHslUV protease complex
B0009408biological_processresponse to heat
B0016787molecular_functionhydrolase activity
B0019904molecular_functionprotein domain specific binding
B0030163biological_processprotein catabolic process
B0030164biological_processprotein denaturation
B0034605biological_processcellular response to heat
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0051603biological_processproteolysis involved in protein catabolic process
C0000287molecular_functionmagnesium ion binding
C0003824molecular_functioncatalytic activity
C0004176molecular_functionATP-dependent peptidase activity
C0004298molecular_functionthreonine-type endopeptidase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005839cellular_componentproteasome core complex
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0009376cellular_componentHslUV protease complex
C0009408biological_processresponse to heat
C0016787molecular_functionhydrolase activity
C0019904molecular_functionprotein domain specific binding
C0030163biological_processprotein catabolic process
C0030164biological_processprotein denaturation
C0034605biological_processcellular response to heat
C0042802molecular_functionidentical protein binding
C0046872molecular_functionmetal ion binding
C0051603biological_processproteolysis involved in protein catabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00248, ECO:0000269|PubMed:9257689
ChainResidueDetails
ATHR2
BTHR2
CTHR2

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AASP164
AILE167
AASN170
BASP164
BILE167
BASN170
CASP164
CILE167
CASN170

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
AGLY47
ALYS33
ATHR1
ASER129

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
BGLY47
BLYS33
BTHR1
BSER129

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
CGLY47
CLYS33
CTHR1
CSER129

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
AGLY44
ALYS33
ATHR1
ASER129

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
BGLY44
BLYS33
BTHR1
BSER129

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
CGLY44
CLYS33
CTHR1
CSER129

site_idMCSA1
Number of Residues4
DetailsM-CSA 678
ChainResidueDetails
ATHR1proton acceptor, proton donor
ALYS33electrostatic stabiliser
AGLY44electrostatic stabiliser
ASER129electrostatic stabiliser

site_idMCSA2
Number of Residues4
DetailsM-CSA 678
ChainResidueDetails
BTHR1proton acceptor, proton donor
BLYS33electrostatic stabiliser
BGLY44electrostatic stabiliser
BSER129electrostatic stabiliser

site_idMCSA3
Number of Residues4
DetailsM-CSA 678
ChainResidueDetails
CTHR1proton acceptor, proton donor
CLYS33electrostatic stabiliser
CGLY44electrostatic stabiliser
CSER129electrostatic stabiliser

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PDB entries from 2025-06-11

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