2L6L

Solution structure of human J-protein co-chaperone, Dph4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001671	molecular_function	ATPase activator activity
A	0005737	cellular_component	cytoplasm
A	0005856	cellular_component	cytoskeleton
A	0008198	molecular_function	ferrous iron binding
A	0008270	molecular_function	zinc ion binding
A	0017183	biological_process	protein histidyl modification to diphthamide
A	0032781	biological_process	positive regulation of ATP-dependent activity
A	0046872	molecular_function	metal ion binding
A	0061077	biological_process	chaperone-mediated protein folding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 201

Chain	Residue
A	CYS115
A	CYS117
A	CYS136
A	CYS139

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00456, ECO:0000269|PubMed:22367199

Chain	Residue	Details
A	ARG116
A	ASP137

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00456, ECO:0000269|PubMed:22367199, ECO:0007744|PDB:2L6L

Chain	Residue	Details
A	GLY118
A	SER140

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