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1M4Y

Crystal structure of HslV from Thermotoga maritima

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004298molecular_functionthreonine-type endopeptidase activity
A0005737cellular_componentcytoplasm
A0005839cellular_componentproteasome core complex
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0009376cellular_componentHslUV protease complex
A0016787molecular_functionhydrolase activity
A0030163biological_processprotein catabolic process
A0046872molecular_functionmetal ion binding
A0051603biological_processproteolysis involved in protein catabolic process
B0003824molecular_functioncatalytic activity
B0004298molecular_functionthreonine-type endopeptidase activity
B0005737cellular_componentcytoplasm
B0005839cellular_componentproteasome core complex
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0009376cellular_componentHslUV protease complex
B0016787molecular_functionhydrolase activity
B0030163biological_processprotein catabolic process
B0046872molecular_functionmetal ion binding
B0051603biological_processproteolysis involved in protein catabolic process
C0003824molecular_functioncatalytic activity
C0004298molecular_functionthreonine-type endopeptidase activity
C0005737cellular_componentcytoplasm
C0005839cellular_componentproteasome core complex
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0009376cellular_componentHslUV protease complex
C0016787molecular_functionhydrolase activity
C0030163biological_processprotein catabolic process
C0046872molecular_functionmetal ion binding
C0051603biological_processproteolysis involved in protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA C 250
ChainResidue
CGLY156
CCYS159
CTHR162
CHOH268
CHOH288
CHOH301

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 251
ChainResidue
BHOH253
BHOH271
BHOH290
BGLY156
BCYS159
BTHR162

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 252
ChainResidue
AGLY156
ACYS159
ATHR162
AHOH257
AHOH273
AHOH294

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12646382","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
AGLY48
ALYS33
ATHR1
ASER124

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
BGLY48
BLYS33
BTHR1
BSER124

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
CGLY48
CLYS33
CTHR1
CSER124

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
AGLY45
ALYS33
ATHR1
ASER124

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
BGLY45
BLYS33
BTHR1
BSER124

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
CGLY45
CLYS33
CTHR1
CSER124

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PDB entries from 2025-10-08

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