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3TX7

Crystal structure of LRH-1/beta-catenin complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0045296molecular_functioncadherin binding
B0003677molecular_functionDNA binding
B0004879molecular_functionnuclear receptor activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE P6L B 100
ChainResidue
BTHR341
BGLN419
BALA420
BGLY421
BTHR423
BLEU424
BMET428
BALA513
BTYR516
BLEU517
BLYS520
BPHE342
BMET345
BTRP382
BSER383
BLEU386
BILE387
BHIS390
BILE416

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15897460
ChainResidueDetails
BLYS520
BGLY421
BTYR516

site_idSWS_FT_FI2
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000269|PubMed:20159957
ChainResidueDetails
BLYS270

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CDK5 => ECO:0000269|PubMed:17009320
ChainResidueDetails
ASER246

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by PTK6 => ECO:0000269|PubMed:20026641
ChainResidueDetails
ATYR331

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by SRC and PTK6 => ECO:0000269|PubMed:22056988, ECO:0000305|PubMed:20026641
ChainResidueDetails
ATYR333

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER552

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18220336
ChainResidueDetails
ATHR556

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q02248
ChainResidueDetails
ACYS619

221051

PDB entries from 2024-06-12

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