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4DNK

Crystal structure of a tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta polypeptide (YWHAB) from homo sapiens at 2.20 A resolution.

Functional Information from GO Data
ChainGOidnamespacecontents
A0004860molecular_functionprotein kinase inhibitor activity
A0004864molecular_functionprotein phosphatase inhibitor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005774cellular_componentvacuolar membrane
A0005829cellular_componentcytosol
A0005925cellular_componentfocal adhesion
A0006605biological_processprotein targeting
A0007165biological_processsignal transduction
A0008104biological_processintracellular protein localization
A0016020cellular_componentmembrane
A0017053cellular_componenttranscription repressor complex
A0019899molecular_functionenzyme binding
A0019904molecular_functionprotein domain specific binding
A0032991cellular_componentprotein-containing complex
A0035332biological_processpositive regulation of hippo signaling
A0042308biological_processnegative regulation of protein import into nucleus
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0042826molecular_functionhistone deacetylase binding
A0044877molecular_functionprotein-containing complex binding
A0045296molecular_functioncadherin binding
A0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
A0045892biological_processnegative regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0048471cellular_componentperinuclear region of cytoplasm
A0050815molecular_functionphosphoserine residue binding
A0051219molecular_functionphosphoprotein binding
A0060243biological_processnegative regulation of cell growth involved in contact inhibition
A0070062cellular_componentextracellular exosome
A0140311molecular_functionprotein sequestering activity
B0004860molecular_functionprotein kinase inhibitor activity
B0004864molecular_functionprotein phosphatase inhibitor activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005774cellular_componentvacuolar membrane
B0005829cellular_componentcytosol
B0005925cellular_componentfocal adhesion
B0006605biological_processprotein targeting
B0007165biological_processsignal transduction
B0008104biological_processintracellular protein localization
B0016020cellular_componentmembrane
B0017053cellular_componenttranscription repressor complex
B0019899molecular_functionenzyme binding
B0019904molecular_functionprotein domain specific binding
B0032991cellular_componentprotein-containing complex
B0035332biological_processpositive regulation of hippo signaling
B0042308biological_processnegative regulation of protein import into nucleus
B0042470cellular_componentmelanosome
B0042802molecular_functionidentical protein binding
B0042826molecular_functionhistone deacetylase binding
B0044877molecular_functionprotein-containing complex binding
B0045296molecular_functioncadherin binding
B0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
B0045892biological_processnegative regulation of DNA-templated transcription
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0048471cellular_componentperinuclear region of cytoplasm
B0050815molecular_functionphosphoserine residue binding
B0051219molecular_functionphosphoprotein binding
B0060243biological_processnegative regulation of cell growth involved in contact inhibition
B0070062cellular_componentextracellular exosome
B0140311molecular_functionprotein sequestering activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 301
ChainResidue
AARG85
AGLU89
AVAL134
AALA135
ASER136

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 302
ChainResidue
AARG20
ATYR21
AASP22
AASP23

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 303
ChainResidue
ALYS159
AARG169
AGLU200

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 304
ChainResidue
AASN185
BLYS70

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 305
ChainResidue
ALYS51
AGLY55
AARG58
ATYR130
AHOH493

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE PO4 B 301
ChainResidue
BTHR2
BGLU7
BASP225

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 B 302
ChainResidue
BARG85
BGLU89
BVAL134
BALA135
BSER136

Functional Information from PROSITE/UniProt
site_idPS00796
Number of Residues11
Details1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
ChainResidueDetails
AARG43-VAL53

site_idPS00797
Number of Residues20
Details1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
ChainResidueDetails
ATYR213-SER232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSite: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"Q9CQV8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68251","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P27348","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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