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3M50

Structure of the 14-3-3/PMA2 complex stabilized by Epibestatin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0007165biological_processsignal transduction
A0008104biological_processprotein localization
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EBT A 241
ChainResidue
AVAL53
ALYS56
AASN57
AHOH258
PLEU929
PHIS930
PHIS935
PILE956

Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG48-VAL58

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR220-SER239

219869

PDB entries from 2024-05-15

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