4NKG

Crystal structure of SspH1 LRR domain in complex PKN1 HR1b domain

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0007165	biological_process	signal transduction
D	0007165	biological_process	signal transduction

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HEZ A 501

Chain	Residue
A	SER305
A	TRP323
A	TYR325
B	ASP178

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HEZ C 501

Chain	Residue
C	TRP263
C	SER285
C	ARG303
D	ASP178

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	Repeat: {"description":"LRR 1"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	36
Details	Repeat: {"description":"LRR 2"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	42
Details	Repeat: {"description":"LRR 3"}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	34
Details	Repeat: {"description":"LRR 4"}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	42
Details	Repeat: {"description":"LRR 5"}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	34
Details	Repeat: {"description":"LRR 6"}

Chain

Residue

Details

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site_id	SWS_FT_FI7
Number of Residues	44
Details	Repeat: {"description":"LRR 7"}

Chain

Residue

Details

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site_id	SWS_FT_FI8
Number of Residues	40
Details	Repeat: {"description":"LRR 8"}

Chain

Residue

Details

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site_id	SWS_FT_FI9
Number of Residues	8
Details	Region: {"description":"Important for interaction with bacterial SspH1 and SspH1-mediated polyubiquitination","evidences":[{"source":"PubMed","id":"24248594","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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