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5F0P

Structure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1(L557M) (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
AALA101
AGLY102
AEDO509

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
AGLU288
AHIS290
AARG254

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

site_idAC6
Number of Residues7
Detailsbinding site for residue EDO A 506
ChainResidue
ACYS137
AVAL140
AGLN141
AARG150
AGLU189
ALYS192
BGLU244

site_idAC7
Number of Residues2
Detailsbinding site for residue EDO A 507
ChainResidue
AASN294
ALYS296

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

site_idAC9
Number of Residues1
Detailsbinding site for residue EDO A 509
ChainResidue
ASO4502

site_idAD1
Number of Residues3
Detailsbinding site for residue EDO A 510
ChainResidue
AHIS387
AASP429
AARG433

site_idAD2
Number of Residues2
Detailsbinding site for residue EDO A 511
ChainResidue
ALYS120
AASN159

site_idAD3
Number of Residues2
Detailsbinding site for residue EDO A 512
ChainResidue
AARG204
CARG52

site_idAD4
Number of Residues4
Detailsbinding site for residue SO4 B 401
ChainResidue
BTYR118
BASP263
BVAL264
BASN265

site_idAD5
Number of Residues4
Detailsbinding site for residue GOL B 402
ChainResidue
BPRO158
BASP159
BVAL160
BLYS184

site_idAD6
Number of Residues1
Detailsbinding site for residue EDO B 403
ChainResidue
BTHR156

site_idAD7
Number of Residues5
Detailsbinding site for residue EDO B 404
ChainResidue
BMSE26
BHIS39
BTYR40
BTYR147
BASP148

site_idAD8
Number of Residues2
Detailsbinding site for residue EDO B 405
ChainResidue
BARG69
BGLU94

site_idAD9
Number of Residues4
Detailsbinding site for residue EDO B 406
ChainResidue
BLYS213
BGLU215
BGLU226
BGLU228

site_idAE1
Number of Residues8
Detailsbinding site for residue EDO B 407
ChainResidue
BGLU77
BLEU78
BPHE79
BASN80
BALA124
BASN125
BVAL126
BARG127

site_idAE2
Number of Residues5
Detailsbinding site for residue EDO B 408
ChainResidue
BILE216
BGLY218
BASP263
BPHE268
BSER269

site_idAE3
Number of Residues4
Detailsbinding site for residue EDO B 409
ChainResidue
BGLN153
BALA155
BPRO259
BARG296

site_idAE4
Number of Residues4
Detailsbinding site for residue EDO B 410
ChainResidue
BLYS82
BASN162
BSER163
BEDO411

site_idAE5
Number of Residues5
Detailsbinding site for residue EDO B 411
ChainResidue
BASN80
BVAL160
BASN161
BASN162
BEDO410

site_idAE6
Number of Residues5
Detailsbinding site for residue EDO B 412
ChainResidue
BASP81
BASN84
BTYR157
BLYS182
BHIS186

site_idAE7
Number of Residues2
Detailsbinding site for residue EDO B 413
ChainResidue
BLYS214
BTHR225

site_idAE8
Number of Residues5
Detailsbinding site for residue GOL B 414
ChainResidue
BLEU199
BVAL200
BARG201
BLYS242
CSER26

site_idAE9
Number of Residues4
Detailsbinding site for residue ZN B 415
ChainResidue
BGLU167
BHIS175
DHIS563
DHIS565

site_idAF1
Number of Residues5
Detailsbinding site for residue SO4 C 201
ChainResidue
CSO4202
CPHE46
CARG70
CTYR71
CSER72

site_idAF2
Number of Residues6
Detailsbinding site for residue SO4 C 202
ChainResidue
CLYS95
CALA96
CGLN100
CILE109
CARG118
CSO4201

site_idAF3
Number of Residues4
Detailsbinding site for residue SO4 C 203
ChainResidue
CSER34
CASN35
CPRO36
CLYS119

site_idAF4
Number of Residues2
Detailsbinding site for residue EDO C 204
ChainResidue
CLYS63
CGLU64

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

222926

PDB entries from 2024-07-24

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