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5F0M

Structure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1 (SeMet labeled)

Functional Information from GO Data
ChainGOidnamespacecontents
A0015031biological_processprotein transport
A0030906cellular_componentretromer, cargo-selective complex
A0042147biological_processretrograde transport, endosome to Golgi
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005768cellular_componentendosome
B0005769cellular_componentearly endosome
B0005829cellular_componentcytosol
B0006886biological_processintracellular protein transport
B0010008cellular_componentendosome membrane
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0016241biological_processregulation of macroautophagy
B0030904cellular_componentretromer complex
B0030906cellular_componentretromer, cargo-selective complex
B0031982cellular_componentvesicle
B0032456biological_processendocytic recycling
B0042147biological_processretrograde transport, endosome to Golgi
B0097422cellular_componenttubular endosome
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005768cellular_componentendosome
C0005769cellular_componentearly endosome
C0005829cellular_componentcytosol
C0008289molecular_functionlipid binding
C0009617biological_processresponse to bacterium
C0010008cellular_componentendosome membrane
C0010314molecular_functionphosphatidylinositol-5-phosphate binding
C0010324biological_processmembrane invagination
C0010976biological_processpositive regulation of neuron projection development
C0015031biological_processprotein transport
C0019903molecular_functionprotein phosphatase binding
C0022615biological_processprotein to membrane docking
C0030111biological_processregulation of Wnt signaling pathway
C0030136cellular_componentclathrin-coated vesicle
C0030904cellular_componentretromer complex
C0031901cellular_componentearly endosome membrane
C0032009cellular_componentearly phagosome
C0032266molecular_functionphosphatidylinositol-3-phosphate binding
C0032456biological_processendocytic recycling
C0034499biological_processlate endosome to Golgi transport
C0035091molecular_functionphosphatidylinositol binding
C0042177biological_processnegative regulation of protein catabolic process
C0045335cellular_componentphagocytic vesicle
C0046597biological_processnegative regulation of viral entry into host cell
C0050765biological_processnegative regulation of phagocytosis
C0051224biological_processnegative regulation of protein transport
C0070062cellular_componentextracellular exosome
C0070273molecular_functionphosphatidylinositol-4-phosphate binding
C0070676biological_processintralumenal vesicle formation
C0080025molecular_functionphosphatidylinositol-3,5-bisphosphate binding
C1901981molecular_functionphosphatidylinositol phosphate binding
C1905394molecular_functionretromer complex binding
C2000642biological_processnegative regulation of early endosome to late endosome transport
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue SO4 A 501
ChainResidue
AARG54

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 502
ChainResidue
ATYR100
AALA101
AGLY102

site_idAC3
Number of Residues4
Detailsbinding site for residue GOL A 503
ChainResidue
ALYS38
ALEU39
AMET40
AASP41

site_idAC4
Number of Residues3
Detailsbinding site for residue GOL A 504
ChainResidue
ACYS156
AASN159
ALYS120

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO A 505
ChainResidue
AARG54
AILE105
BGLU234
BASP237

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 506
ChainResidue
AARG254
AGLU288
AHIS290

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO A 507
ChainResidue
ASER56
AHIS142

site_idAC8
Number of Residues1
Detailsbinding site for residue EDO A 508
ChainResidue
AARG365

site_idAC9
Number of Residues5
Detailsbinding site for residue SO4 B 401
ChainResidue
BTYR118
BASP263
BVAL264
BASN265
BLYS266

site_idAD1
Number of Residues4
Detailsbinding site for residue GOL B 402
ChainResidue
BPRO158
BASP159
BVAL160
BLYS184

site_idAD2
Number of Residues5
Detailsbinding site for residue EDO B 403
ChainResidue
BLYS38
BHIS39
BTYR40
BTYR147
BASP148

site_idAD3
Number of Residues3
Detailsbinding site for residue EDO B 404
ChainResidue
BARG69
BGLU94
BVAL137

site_idAD4
Number of Residues6
Detailsbinding site for residue EDO B 405
ChainResidue
BGLU77
BLEU78
BPHE79
BASN80
BALA124
BARG127

site_idAD5
Number of Residues4
Detailsbinding site for residue EDO B 406
ChainResidue
BILE216
BASP263
BPHE268
BSER269

site_idAD6
Number of Residues6
Detailsbinding site for residue EDO B 407
ChainResidue
BGLN153
BLEU154
BALA155
BPRO259
BTRP295
BARG296

site_idAD7
Number of Residues1
Detailsbinding site for residue EDO B 408
ChainResidue
BLYS214

site_idAD8
Number of Residues3
Detailsbinding site for residue EDO B 409
ChainResidue
BTYR157
BLYS182
BHIS186

site_idAD9
Number of Residues5
Detailsbinding site for residue SO4 C 201
ChainResidue
CPHE46
CARG70
CTYR71
CSER72
CSO4202

site_idAE1
Number of Residues6
Detailsbinding site for residue SO4 C 202
ChainResidue
CLYS95
CALA96
CGLN100
CILE109
CARG118
CSO4201

site_idAE2
Number of Residues4
Detailsbinding site for residue SO4 C 203
ChainResidue
CSER34
CASN35
CPRO36
CLYS119

site_idAE3
Number of Residues4
Detailsbinding site for residue GOL C 204
ChainResidue
BLEU199
BARG201
BLYS242
CSER26

site_idAE4
Number of Residues2
Detailsbinding site for residue GOL C 205
ChainResidue
CLEU62
CLYS63

site_idAE5
Number of Residues3
Detailsbinding site for residue EDO C 206
ChainResidue
CARG99
CLEU101
CASP106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
CARG70
CSER72
CLYS95
CARG118

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
CALA2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine => ECO:0007744|PubMed:24129315
ChainResidueDetails
CARG43

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER72

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS95

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PDB entries from 2024-11-06

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