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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
A0035332biological_processpositive regulation of hippo signaling
A0035580cellular_componentspecific granule lumen
A0040001biological_processestablishment of mitotic spindle localization
A0042564cellular_componentNLS-dependent protein nuclear import complex
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0045893biological_processpositive regulation of DNA-templated transcription
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
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
B0008270molecular_functionzinc ion binding
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
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
B0048762biological_processmesenchymal cell differentiation
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 Residues80
DetailsDomain: {"description":"Importin N-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00115","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsRepeat: {"description":"HEAT 2","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues38
DetailsRepeat: {"description":"HEAT 3","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues31
DetailsRepeat: {"description":"HEAT 4","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues32
DetailsRepeat: {"description":"HEAT 5","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues35
DetailsRepeat: {"description":"HEAT 6","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues49
DetailsRepeat: {"description":"HEAT 7","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues46
DetailsRepeat: {"description":"HEAT 8","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues30
DetailsRepeat: {"description":"HEAT 9","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues36
DetailsRepeat: {"description":"HEAT 10","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10367892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues36
DetailsRepeat: {"description":"HEAT 11","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues37
DetailsRepeat: {"description":"HEAT 12","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues48
DetailsRepeat: {"description":"HEAT 13","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues39
DetailsRepeat: {"description":"HEAT 14","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues37
DetailsRepeat: {"description":"HEAT 15","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues38
DetailsRepeat: {"description":"HEAT 16","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues44
DetailsRepeat: {"description":"HEAT 17","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues43
DetailsRepeat: {"description":"HEAT 18","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues42
DetailsRepeat: {"description":"HEAT 19","evidences":[{"source":"PubMed","id":"10353244","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues176
DetailsRegion: {"description":"Essential for high affinity interaction with RPL23A","evidences":[{"source":"PubMed","id":"9687515","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues13
DetailsRegion: {"description":"IAB-binding"}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues85
DetailsRegion: {"description":"Ran-GTP binding"}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues22
DetailsZinc finger: {"description":"C2H2-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues24
DetailsZinc finger: {"description":"C2H2-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues22
DetailsZinc finger: {"description":"C2H2-type 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues23
DetailsZinc finger: {"description":"C2H2-type 4; atypical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00042","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by LATS2","evidences":[{"source":"PubMed","id":"21952048","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PAK1","evidences":[{"source":"PubMed","id":"15833848","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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