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8X7V

Structure of human SCMC ternary complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005938cellular_componentcell cortex
A0006887biological_processexocytosis
A0006974biological_processDNA damage response
A0007015biological_processactin filament organization
A0008643biological_processcarbohydrate transport
A0015144molecular_functioncarbohydrate transmembrane transporter activity
A0015631molecular_functiontubulin binding
A0015768biological_processmaltose transport
A0016020cellular_componentmembrane
A0030288cellular_componentouter membrane-bounded periplasmic space
A0031410cellular_componentcytoplasmic vesicle
A0032880biological_processregulation of protein localization
A0034219biological_processcarbohydrate transmembrane transport
A0034289biological_processdetection of maltose stimulus
A0040019biological_processpositive regulation of embryonic development
A0042597cellular_componentperiplasmic space
A0042956biological_processmaltodextrin transmembrane transport
A0043190cellular_componentATP-binding cassette (ABC) transporter complex
A0050727biological_processregulation of inflammatory response
A0051293biological_processestablishment of spindle localization
A0051302biological_processregulation of cell division
A0051656biological_processestablishment of organelle localization
A0055052cellular_componentATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing
A0055085biological_processtransmembrane transport
A0060326biological_processcell chemotaxis
A0060471biological_processcortical granule exocytosis
A0060473cellular_componentcortical granule
A0106333cellular_componentsubcortical maternal complex
A0140089biological_processprotein storage
A0140094molecular_functionstructural constituent of cytoplasmic lattice
A0140095cellular_componentcytoplasmic lattice
A1901982molecular_functionmaltose binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005938cellular_componentcell cortex
B0007015biological_processactin filament organization
B0009880biological_processembryonic pattern specification
B0031297biological_processreplication fork processing
B0032880biological_processregulation of protein localization
B0032991cellular_componentprotein-containing complex
B0035088biological_processestablishment or maintenance of apical/basal cell polarity
B0040019biological_processpositive regulation of embryonic development
B0045836biological_processpositive regulation of meiotic nuclear division
B0051293biological_processestablishment of spindle localization
B0051302biological_processregulation of cell division
B0070201biological_processregulation of establishment of protein localization
B0106333cellular_componentsubcortical maternal complex
B0140089biological_processprotein storage
B0140094molecular_functionstructural constituent of cytoplasmic lattice
B0140095cellular_componentcytoplasmic lattice
B1905168biological_processpositive regulation of double-strand break repair via homologous recombination
B2000781biological_processpositive regulation of double-strand break repair
C0000794cellular_componentcondensed nuclear chromosome
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005940cellular_componentseptin ring
C0006355biological_processregulation of DNA-templated transcription
C0016925biological_processprotein sumoylation
C0031386molecular_functionprotein tag activity
C0042802molecular_functionidentical protein binding
C0044389molecular_functionubiquitin-like protein ligase binding
Functional Information from PROSITE/UniProt
site_idPS01037
Number of Residues18
DetailsSBP_BACTERIAL_1 Bacterial extracellular solute-binding proteins, family 1 signature. PIAvEalSLIYNkdlLpN
ChainResidueDetails
APRO-202-ASN-185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues23
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues23
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues23
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues27
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues27
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues23
DetailsRepeat: {"description":"LRR 7"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues23
DetailsRepeat: {"description":"LRR 8"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues23
DetailsRepeat: {"description":"LRR 9"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues27
DetailsRepeat: {"description":"LRR 10"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues23
DetailsRepeat: {"description":"LRR 11"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues28
DetailsRepeat: {"description":"LRR 12"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues21
DetailsRepeat: {"description":"LRR 13"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues10
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00136","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues61
DetailsDomain: {"description":"KH; atypical"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues38
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues40
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues39
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues37
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues39
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues39
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues31
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"26537248","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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