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1JJW

Structure of Haemophilus influenzae HslV Protein at 1.9 A Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0004298molecular_functionthreonine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005839cellular_componentproteasome core complex
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0009376cellular_componentHslUV protease complex
A0030163biological_processprotein catabolic process
A0046872molecular_functionmetal ion binding
A0051603biological_processproteolysis involved in protein catabolic process
B0004298molecular_functionthreonine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005839cellular_componentproteasome core complex
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0009376cellular_componentHslUV protease complex
B0030163biological_processprotein catabolic process
B0046872molecular_functionmetal ion binding
B0051603biological_processproteolysis involved in protein catabolic process
C0004298molecular_functionthreonine-type endopeptidase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005839cellular_componentproteasome core complex
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0009376cellular_componentHslUV protease complex
C0030163biological_processprotein catabolic process
C0046872molecular_functionmetal ion binding
C0051603biological_processproteolysis involved in protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K A 501
ChainResidue
AGLY157
ACYS160
ATHR163
AHOH236
AHOH237
AHOH238
BHOH346

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 502
ChainResidue
BCYS160
BTHR163
BHOH334
BHOH336
AHOH335
BGLY157

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K C 503
ChainResidue
CGLY157
CCYS160
CTHR163
CHOH438
CHOH439
CHOH454

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE:
ChainResidueDetails
ATHR2
BTHR2
CTHR2

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AASP158
AVAL161
AASN164
BASP158
BVAL161
BASN164
CASP158
CVAL161
CASN164

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
AGLY48
ALYS33
ATHR1
ASER125

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
BGLY48
BLYS33
BTHR1
BSER125

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
CGLY48
CLYS33
CTHR1
CSER125

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
AGLY45
ALYS33
ATHR1
ASER125

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
BGLY45
BLYS33
BTHR1
BSER125

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1pma
ChainResidueDetails
CGLY45
CLYS33
CTHR1
CSER125

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PDB entries from 2024-09-11

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