6HB1

Structure of Hgh1, crystal form I

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0006458	biological_process	'de novo' protein folding
A	0030674	molecular_function	protein-macromolecule adaptor activity
A	0061770	molecular_function	translation elongation factor binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0006458	biological_process	'de novo' protein folding
B	0030674	molecular_function	protein-macromolecule adaptor activity
B	0061770	molecular_function	translation elongation factor binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0006458	biological_process	'de novo' protein folding
C	0030674	molecular_function	protein-macromolecule adaptor activity
C	0061770	molecular_function	translation elongation factor binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0006458	biological_process	'de novo' protein folding
D	0030674	molecular_function	protein-macromolecule adaptor activity
D	0061770	molecular_function	translation elongation factor binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue CL A 401

Chain	Residue
A	LYS225
A	VAL226
A	HOH572
D	ASN26

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site_id	AC2
Number of Residues	3
Details	binding site for residue CL C 401

Chain	Residue
B	ASN26
C	LYS225
C	VAL226

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site_id	AC3
Number of Residues	3
Details	binding site for residue CL D 401

Chain	Residue
D	ASN83
C	LYS194
D	LYS79

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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