6GQS

Structure of human Heat shock protein 90-alpha N-terminal domain (Hsp90-NTD) variant K112R in complex with AMPCP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	binding site for residue A12 A 301

Chain	Residue
A	ASN51
A	GLY137
A	PHE138
A	THR184
A	MG303
A	HOH406
A	HOH424
A	HOH450
A	HOH452
A	HOH456
A	HOH461
A	ALA55
A	HOH467
A	HOH480
A	HOH481
A	HOH527
A	HOH536
A	HOH572
A	HOH634
A	ASP93
A	MET98
A	ASN106
A	LEU107
A	ARG112
A	GLY135
A	VAL136

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site_id	AC2
Number of Residues	3
Details	binding site for residue MG A 302

Chain	Residue
A	HOH462
A	HOH468
A	HOH579

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site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 303

Chain	Residue
A	ASN51
A	A12301
A	HOH452
A	HOH467
A	HOH480

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Functional Information from PROSITE/UniProt

site_id	PS00298
Number of Residues	10
Details	HSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE

Chain	Residue	Details
A	TYR38-GLU47

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by PRKDC","evidences":[{"source":"PubMed","id":"2507541","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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