4DJS

Structure of beta-catenin in complex with a stapled peptide inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0007155	biological_process	cell adhesion
A	0045296	molecular_function	cadherin binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR CHAIN B OF STAPLED PEPTIDE

Chain	Residue
A	HIS219
A	ASP299
A	LYS335
A	GLU479
A	ASN483
A	ARG486
A	PRO521
A	GLU642
A	ARG647
A	HIS223
A	PHE253
A	THR257
A	HIS260
A	ASN261
A	ASN290
A	LYS292
A	ILE296

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CDK5 => ECO:0000269|PubMed:17009320, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER191

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CDK5 => ECO:0000269|PubMed:17009320

Chain	Residue	Details
A	SER246

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by PTK6 => ECO:0000269|PubMed:20026641

Chain	Residue	Details
A	TYR331

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphotyrosine; by SRC and PTK6 => ECO:0000269|PubMed:22056988, ECO:0000305|PubMed:20026641

Chain	Residue	Details
A	TYR333

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER552

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18220336

Chain	Residue	Details
A	THR556

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q02248

Chain	Residue	Details
A	CYS619

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