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3BVO

Crystal structure of human co-chaperone protein HscB

Functional Information from GO Data
ChainGOidnamespacecontents
A0001671molecular_functionATPase activator activity
A0044571biological_process[2Fe-2S] cluster assembly
A0051087molecular_functionprotein-folding chaperone binding
A0051259biological_processprotein complex oligomerization
B0001671molecular_functionATPase activator activity
B0044571biological_process[2Fe-2S] cluster assembly
B0051087molecular_functionprotein-folding chaperone binding
B0051259biological_processprotein complex oligomerization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 301
ChainResidue
ACYS41
ACYS44
ACYS58
ACYS61

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 301
ChainResidue
BCYS41
BASN43
BCYS44
BCYS58
BCYS61

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
ASER82
APHE83
AARG84
APHE203
AGLU204

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:18713742, ECO:0007744|PDB:3BVO
ChainResidueDetails
ACYS41
ACYS44
ACYS58
ACYS61
BCYS41
BCYS44
BCYS58
BCYS61

225158

PDB entries from 2024-09-18

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