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1G41

CRYSTAL STRUCTURE OF HSLU HAEMOPHILUS INFLUENZAE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0008233molecular_functionpeptidase activity
A0009376cellular_componentHslUV protease complex
A0010498biological_processproteasomal protein catabolic process
A0016887molecular_functionATP hydrolysis activity
A0036402molecular_functionproteasome-activating activity
A0043335biological_processprotein unfolding
A0051603biological_processproteolysis involved in protein catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 600
ChainResidue
AGLU342
ATHR370
ATHR371
ALYS375
AASP422
AALA423
AHOH511

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP A 450
ChainResidue
AILE18
APRO58
ATHR59
AGLY60
AVAL61
AGLY62
ALYS63
ATHR64
AGLU65
ALEU336
AALA393
AARG394
AHOH463
AHOH518
AHIS16
AILE17

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11106733","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-11-05

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