2N9P

Solution structure of RNF126 N-terminal zinc finger domain in complex with BAG6 Ubiquitin-like domain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0061630	molecular_function	ubiquitin protein ligase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 101

Chain	Residue
A	CYS13
A	CYS16
A	CYS29
A	CYS32

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Functional Information from PROSITE/UniProt

site_id	PS00299
Number of Residues	26
Details	UBIQUITIN_1 Ubiquitin domain signature. KehIaAsvsIPsekQrLIYqGrvlqD

Chain	Residue	Details
C	LYS43-ASP68

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	19
Details	Zinc finger: {"description":"C4-type","evidences":[{"source":"PubMed","id":"27193484","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"27193484","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2N9O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	75
Details	Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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