5F0J
Structure of retromer VPS26-VPS35 subunits bound to SNX3
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0015031 | biological_process | protein transport |
A | 0030906 | cellular_component | retromer, cargo-selective complex |
A | 0042147 | biological_process | retrograde transport, endosome to Golgi |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005764 | cellular_component | lysosome |
B | 0005768 | cellular_component | endosome |
B | 0005769 | cellular_component | early endosome |
B | 0005829 | cellular_component | cytosol |
B | 0006886 | biological_process | intracellular protein transport |
B | 0010008 | cellular_component | endosome membrane |
B | 0015031 | biological_process | protein transport |
B | 0016020 | cellular_component | membrane |
B | 0016241 | biological_process | regulation of macroautophagy |
B | 0030904 | cellular_component | retromer complex |
B | 0030906 | cellular_component | retromer, cargo-selective complex |
B | 0031982 | cellular_component | vesicle |
B | 0032456 | biological_process | endocytic recycling |
B | 0042147 | biological_process | retrograde transport, endosome to Golgi |
B | 0097422 | cellular_component | tubular endosome |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005768 | cellular_component | endosome |
C | 0005769 | cellular_component | early endosome |
C | 0005829 | cellular_component | cytosol |
C | 0008289 | molecular_function | lipid binding |
C | 0009617 | biological_process | response to bacterium |
C | 0010008 | cellular_component | endosome membrane |
C | 0010314 | molecular_function | phosphatidylinositol-5-phosphate binding |
C | 0010324 | biological_process | membrane invagination |
C | 0010976 | biological_process | positive regulation of neuron projection development |
C | 0015031 | biological_process | protein transport |
C | 0019903 | molecular_function | protein phosphatase binding |
C | 0022615 | biological_process | protein to membrane docking |
C | 0030111 | biological_process | regulation of Wnt signaling pathway |
C | 0030136 | cellular_component | clathrin-coated vesicle |
C | 0030904 | cellular_component | retromer complex |
C | 0031901 | cellular_component | early endosome membrane |
C | 0032009 | cellular_component | early phagosome |
C | 0032266 | molecular_function | phosphatidylinositol-3-phosphate binding |
C | 0032456 | biological_process | endocytic recycling |
C | 0034499 | biological_process | late endosome to Golgi transport |
C | 0035091 | molecular_function | phosphatidylinositol binding |
C | 0042177 | biological_process | negative regulation of protein catabolic process |
C | 0045335 | cellular_component | phagocytic vesicle |
C | 0046597 | biological_process | negative regulation of viral entry into host cell |
C | 0050765 | biological_process | negative regulation of phagocytosis |
C | 0051224 | biological_process | negative regulation of protein transport |
C | 0070062 | cellular_component | extracellular exosome |
C | 0070273 | molecular_function | phosphatidylinositol-4-phosphate binding |
C | 0070676 | biological_process | intralumenal vesicle formation |
C | 0080025 | molecular_function | phosphatidylinositol-3,5-bisphosphate binding |
C | 1901981 | molecular_function | phosphatidylinositol phosphate binding |
C | 1905394 | molecular_function | retromer complex binding |
C | 2000642 | biological_process | negative regulation of early endosome to late endosome transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | binding site for residue SO4 A 501 |
Chain | Residue |
A | ARG54 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | ALA101 |
A | GLY102 |
A | HOH607 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | LYS38 |
A | LEU39 |
A | MET40 |
A | ASP41 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | ILE105 |
B | GLU234 |
B | ASP237 |
A | ARG54 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | GLN155 |
A | ARG158 |
A | ARG226 |
A | GLN229 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | CYS137 |
A | VAL140 |
A | GLN141 |
A | ARG150 |
A | GLU189 |
A | LYS192 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | ASN294 |
A | LYS296 |
site_id | AC8 |
Number of Residues | 2 |
Details | binding site for residue EDO A 508 |
Chain | Residue |
A | ARG254 |
A | HIS290 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue EDO A 509 |
Chain | Residue |
A | ASP304 |
A | SER349 |
A | VAL352 |
A | ASN356 |
A | ARG400 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO A 510 |
Chain | Residue |
A | ARG365 |
A | TYR368 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue EDO A 511 |
Chain | Residue |
A | HOH607 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 512 |
Chain | Residue |
A | LYS120 |
A | ASN159 |
site_id | AD4 |
Number of Residues | 4 |
Details | binding site for residue SO4 B 401 |
Chain | Residue |
B | TYR118 |
B | ASP263 |
B | VAL264 |
B | ASN265 |
site_id | AD5 |
Number of Residues | 4 |
Details | binding site for residue GOL B 402 |
Chain | Residue |
B | PRO158 |
B | ASP159 |
B | VAL160 |
B | LYS184 |
site_id | AD6 |
Number of Residues | 4 |
Details | binding site for residue GOL B 403 |
Chain | Residue |
B | ASN275 |
B | ARG285 |
B | PHE287 |
B | GLU326 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue GOL B 404 |
Chain | Residue |
B | ASP81 |
B | ASN84 |
B | TYR157 |
B | LYS182 |
B | HIS186 |
site_id | AD8 |
Number of Residues | 1 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
B | THR156 |
site_id | AD9 |
Number of Residues | 4 |
Details | binding site for residue EDO B 406 |
Chain | Residue |
B | HIS39 |
B | TYR40 |
B | TYR147 |
B | ASP148 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue EDO B 407 |
Chain | Residue |
B | ARG69 |
B | GLU94 |
site_id | AE2 |
Number of Residues | 4 |
Details | binding site for residue EDO B 408 |
Chain | Residue |
B | LYS213 |
B | GLU215 |
B | GLU226 |
B | GLU228 |
site_id | AE3 |
Number of Residues | 8 |
Details | binding site for residue EDO B 409 |
Chain | Residue |
B | GLU77 |
B | LEU78 |
B | PHE79 |
B | ASN80 |
B | ALA124 |
B | ASN125 |
B | VAL126 |
B | ARG127 |
site_id | AE4 |
Number of Residues | 4 |
Details | binding site for residue EDO B 410 |
Chain | Residue |
B | ILE216 |
B | GLY218 |
B | ASP263 |
B | SER269 |
site_id | AE5 |
Number of Residues | 4 |
Details | binding site for residue EDO B 411 |
Chain | Residue |
B | GLU119 |
B | GLN153 |
B | PRO259 |
B | ARG296 |
site_id | AE6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 412 |
Chain | Residue |
B | LYS82 |
B | ASN162 |
B | SER163 |
B | EDO414 |
site_id | AE7 |
Number of Residues | 1 |
Details | binding site for residue EDO B 413 |
Chain | Residue |
B | ARG139 |
site_id | AE8 |
Number of Residues | 4 |
Details | binding site for residue EDO B 414 |
Chain | Residue |
B | ASN80 |
B | ASN161 |
B | ASN162 |
B | EDO412 |
site_id | AE9 |
Number of Residues | 2 |
Details | binding site for residue EDO B 415 |
Chain | Residue |
B | LYS214 |
B | THR225 |
site_id | AF1 |
Number of Residues | 4 |
Details | binding site for residue EDO C 201 |
Chain | Residue |
A | ASP128 |
A | LYS131 |
C | THR8 |
C | ARG10 |
site_id | AF2 |
Number of Residues | 5 |
Details | binding site for residue SO4 C 202 |
Chain | Residue |
C | HOH308 |
C | ARG70 |
C | TYR71 |
C | SER72 |
C | SO4203 |
site_id | AF3 |
Number of Residues | 6 |
Details | binding site for residue SO4 C 203 |
Chain | Residue |
C | LYS95 |
C | ALA96 |
C | GLN100 |
C | ILE109 |
C | ARG118 |
C | SO4202 |
site_id | AF4 |
Number of Residues | 3 |
Details | binding site for residue SO4 C 204 |
Chain | Residue |
C | SER34 |
C | ASN35 |
C | LYS119 |
site_id | AF5 |
Number of Residues | 4 |
Details | binding site for residue GOL C 205 |
Chain | Residue |
B | LEU199 |
B | ARG201 |
B | LYS242 |
C | SER26 |
site_id | AF6 |
Number of Residues | 4 |
Details | binding site for residue EDO C 206 |
Chain | Residue |
C | THR48 |
C | ARG68 |
C | ASP73 |
C | ILE149 |
site_id | AF7 |
Number of Residues | 2 |
Details | binding site for residue EDO C 207 |
Chain | Residue |
A | ARG204 |
C | ARG52 |
site_id | AF8 |
Number of Residues | 1 |
Details | binding site for residue EDO C 208 |
Chain | Residue |
C | LYS63 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
C | ARG70 | |
C | SER72 | |
C | LYS95 | |
C | ARG118 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylalanine => ECO:0000269|PubMed:12665801, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 |
Chain | Residue | Details |
C | ALA2 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Omega-N-methylarginine => ECO:0007744|PubMed:24129315 |
Chain | Residue | Details |
C | ARG43 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | SER72 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
C | LYS95 |