Research workbench
Crystal structure of mouse VPS29 complexed with MN2+
Analyse Crystal structure of mouse VPS29 complexed with MN2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PSN
- Type
- protein
- Length
- 365 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar protein sorting-associated protein 29
- EC
- 3.1.3.3
- UniProt
- Q9QZ88
- Ligands
- MN
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein 29 (EC 3.1.3.3) | protein | 183 | 14% helix, 38% strand | Q9QZ88 |
| B | Vacuolar protein sorting-associated protein 29 (EC 3.1.3.3) | protein | 182 | 14% helix, 37% strand | Q9QZ88 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1255 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 3PSN · Crystal structure of mouse VPS29 complexed with Mn2+ · the same entry in another collection · chain A against A, TM-score 1.00
- Q9QZ88 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 29… · a predicted model of the same protein · chain B against A, TM-score 0.92
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9QZ88
- Elsewhere: RCSB PDB 3PSN · PDBe 3PSN · UniProt Q9QZ88
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