1Z2W
Crystal structure of mouse Vps29 complexed with Mn2+
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005768 | cellular_component | endosome |
A | 0005829 | cellular_component | cytosol |
A | 0006886 | biological_process | intracellular protein transport |
A | 0006896 | biological_process | Golgi to vacuole transport |
A | 0010008 | cellular_component | endosome membrane |
A | 0015031 | biological_process | protein transport |
A | 0016020 | cellular_component | membrane |
A | 0030904 | cellular_component | retromer complex |
A | 0030906 | cellular_component | retromer, cargo-selective complex |
A | 0032456 | biological_process | endocytic recycling |
A | 0042147 | biological_process | retrograde transport, endosome to Golgi |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
A | 0046872 | molecular_function | metal ion binding |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005768 | cellular_component | endosome |
B | 0005829 | cellular_component | cytosol |
B | 0006886 | biological_process | intracellular protein transport |
B | 0006896 | biological_process | Golgi to vacuole transport |
B | 0010008 | cellular_component | endosome membrane |
B | 0015031 | biological_process | protein transport |
B | 0016020 | cellular_component | membrane |
B | 0030904 | cellular_component | retromer complex |
B | 0030906 | cellular_component | retromer, cargo-selective complex |
B | 0032456 | biological_process | endocytic recycling |
B | 0042147 | biological_process | retrograde transport, endosome to Golgi |
B | 0043231 | cellular_component | intracellular membrane-bounded organelle |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN A 601 |
Chain | Residue |
A | ASP8 |
A | HIS10 |
A | ASN39 |
A | HIS117 |
A | MN602 |
A | HOH603 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN A 602 |
Chain | Residue |
A | HIS115 |
A | MN601 |
A | HOH603 |
A | HOH693 |
A | ASN39 |
A | ASP62 |
A | HIS86 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MN B 701 |
Chain | Residue |
B | ASP8 |
B | HIS10 |
B | ASN39 |
B | HIS117 |
B | MN702 |
B | HOH703 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MN B 702 |
Chain | Residue |
B | ASN39 |
B | ASP62 |
B | HIS86 |
B | HIS115 |
B | MN701 |
B | HOH703 |
B | HOH770 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 501 |
Chain | Residue |
A | LYS81 |
A | ASP107 |
A | VAL108 |
A | ASP109 |
A | LYS127 |
A | LYS181 |
A | HOH724 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 502 |
Chain | Residue |
A | ASP154 |
A | TYR163 |
A | TYR165 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 503 |
Chain | Residue |
B | ASP55 |
B | HIS57 |
B | THR76 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 504 |
Chain | Residue |
B | LEU25 |
B | VAL27 |
B | HOH829 |
B | HOH840 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 505 |
Chain | Residue |
A | PHE119 |
A | GLU120 |
A | ALA121 |
A | PHE122 |
A | HOH698 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP8 | |
B | ASN39 | |
B | ASP62 | |
B | HIS86 | |
B | HIS115 | |
B | HIS117 | |
A | HIS10 | |
A | ASN39 | |
A | ASP62 | |
A | HIS86 | |
A | HIS115 | |
A | HIS117 | |
B | ASP8 | |
B | HIS10 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9UBQ0 |
Chain | Residue | Details |
A | LYS50 | |
B | LYS50 |