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6HB1

Structure of Hgh1, crystal form I

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0061077biological_processchaperone-mediated protein folding
A0061770molecular_functiontranslation elongation factor binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0061077biological_processchaperone-mediated protein folding
B0061770molecular_functiontranslation elongation factor binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0061077biological_processchaperone-mediated protein folding
C0061770molecular_functiontranslation elongation factor binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0061077biological_processchaperone-mediated protein folding
D0061770molecular_functiontranslation elongation factor binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CL A 401
ChainResidue
ALYS225
AVAL226
AHOH572
DASN26

site_idAC2
Number of Residues3
Detailsbinding site for residue CL C 401
ChainResidue
BASN26
CLYS225
CVAL226

site_idAC3
Number of Residues3
Detailsbinding site for residue CL D 401
ChainResidue
DASN83
CLYS194
DLYS79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:22814378
ChainResidueDetails
ATHR2
BTHR2
CTHR2
DTHR2

222926

PDB entries from 2024-07-24

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