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 | 0032991 | cellular_component | protein-containing complex |
| A | 0042147 | biological_process | retrograde transport, endosome to Golgi |
| 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 | 0032991 | cellular_component | protein-containing complex |
| B | 0042147 | biological_process | retrograde transport, endosome to Golgi |
| 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 | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9UBQ0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
