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3W5K

Crystal structure of Snail1 and importin beta complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005643cellular_componentnuclear pore
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006404biological_processRNA import into nucleus
A0006606biological_processprotein import into nucleus
A0006607biological_processNLS-bearing protein import into nucleus
A0006610biological_processribosomal protein import into nucleus
A0006886biological_processintracellular protein transport
A0007079biological_processmitotic chromosome movement towards spindle pole
A0007080biological_processmitotic metaphase chromosome alignment
A0008139molecular_functionnuclear localization sequence binding
A0008270molecular_functionzinc ion binding
A0010494cellular_componentcytoplasmic stress granule
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0019899molecular_functionenzyme binding
A0019904molecular_functionprotein domain specific binding
A0030953biological_processastral microtubule organization
A0031267molecular_functionsmall GTPase binding
A0031965cellular_componentnuclear membrane
A0032991cellular_componentprotein-containing complex
A0035580cellular_componentspecific granule lumen
A0040001biological_processestablishment of mitotic spindle localization
A0042564cellular_componentNLS-dependent protein nuclear import complex
A0051879molecular_functionHsp90 protein binding
A0061608molecular_functionnuclear import signal receptor activity
A0061676molecular_functionimportin-alpha family protein binding
A0070062cellular_componentextracellular exosome
A0071782cellular_componentendoplasmic reticulum tubular network
A0090307biological_processmitotic spindle assembly
A1904813cellular_componentficolin-1-rich granule lumen
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000977molecular_functionRNA polymerase II transcription regulatory region sequence-specific DNA binding
B0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
B0000981molecular_functionDNA-binding transcription factor activity, RNA polymerase II-specific
B0001227molecular_functionDNA-binding transcription repressor activity, RNA polymerase II-specific
B0001649biological_processosteoblast differentiation
B0001650cellular_componentfibrillar center
B0001707biological_processmesoderm formation
B0001837biological_processepithelial to mesenchymal transition
B0003180biological_processaortic valve morphogenesis
B0003198biological_processepithelial to mesenchymal transition involved in endocardial cushion formation
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005721cellular_componentpericentric heterochromatin
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006355biological_processregulation of DNA-templated transcription
B0006357biological_processregulation of transcription by RNA polymerase II
B0007219biological_processNotch signaling pathway
B0007498biological_processmesoderm development
B0010631biological_processepithelial cell migration
B0010718biological_processpositive regulation of epithelial to mesenchymal transition
B0010957biological_processnegative regulation of vitamin D biosynthetic process
B0019900molecular_functionkinase binding
B0030335biological_processpositive regulation of cell migration
B0031069biological_processhair follicle morphogenesis
B0043231cellular_componentintracellular membrane-bounded organelle
B0043518biological_processnegative regulation of DNA damage response, signal transduction by p53 class mediator
B0043565molecular_functionsequence-specific DNA binding
B0045892biological_processnegative regulation of DNA-templated transcription
B0045893biological_processpositive regulation of DNA-templated transcription
B0046872molecular_functionmetal ion binding
B0060021biological_processroof of mouth development
B0060070biological_processcanonical Wnt signaling pathway
B0060536biological_processcartilage morphogenesis
B0060707biological_processtrophoblast giant cell differentiation
B0060806biological_processnegative regulation of cell differentiation involved in embryonic placenta development
B0060972biological_processleft/right pattern formation
B0070828biological_processheterochromatin organization
B0070888molecular_functionE-box binding
B1902230biological_processnegative regulation of intrinsic apoptotic signaling pathway in response to DNA damage
B1990837molecular_functionsequence-specific double-stranded DNA binding
B2000810biological_processregulation of bicellular tight junction assembly
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 501
ChainResidue
BCYS156
BCYS159
BLYS161
BHIS172
BHIS176

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 502
ChainResidue
BHIS202
BCYS182
BTHR184
BCYS185
BHIS198

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 503
ChainResidue
BCYS210
BCYS213
BHIS226
BHIS230

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 504
ChainResidue
BCYS238
BCYS241
BHIS254
BCYS259

Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues21
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cky..CnkeYlslgalkmHirs..H
ChainResidueDetails
BCYS156-HIS176
BCYS180-HIS202
BCYS210-HIS230

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsZN_FING: C2H2-type 1 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
BPHE154-HIS176

site_idSWS_FT_FI2
Number of Residues24
DetailsZN_FING: C2H2-type 2 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
BLEU178-HIS202

site_idSWS_FT_FI3
Number of Residues22
DetailsZN_FING: C2H2-type 3 => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
BPHE208-HIS230
ALYS835
ALYS867

site_idSWS_FT_FI4
Number of Residues23
DetailsZN_FING: C2H2-type 4; atypical => ECO:0000255|PROSITE-ProRule:PRU00042
ChainResidueDetails
BTYR236-CYS259

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:19923321
ChainResidueDetails
BSER11

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:19923321
ChainResidueDetails
BSER82

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:19923321
ChainResidueDetails
BSER92

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20305697, ECO:0000305|PubMed:15448698
ChainResidueDetails
BSER96

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000305|PubMed:15448698
ChainResidueDetails
BSER100
BSER111
BSER115
BSER119

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15647282, ECO:0000269|PubMed:19923321, ECO:0000305|PubMed:15448698
ChainResidueDetails
BSER104
BSER107

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by LATS2 => ECO:0000269|PubMed:21952048
ChainResidueDetails
BTHR203

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PAK1 => ECO:0000269|PubMed:15833848
ChainResidueDetails
BSER246

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:20959806
ChainResidueDetails
BSER112

site_idSWS_FT_FI14
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
ChainResidueDetails
BLYS98
BLYS137
BLYS146

218853

PDB entries from 2024-04-24

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