Research workbench
Crystal structure of human prolidase G278N variant expressed in the presence of chaperones
Analyse Crystal structure of human prolidase G278N variant expressed in the presence of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SRF
- Type
- protein
- Length
- 965 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Xaa-pro dipeptidase
- EC
- 3.4.13.9
- UniProt
- P12955
- Ligands
- MN, NA
- Pockets
- 9 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Xaa-pro dipeptidase (EC 3.4.13.9) | protein | 484 | 38% helix, 16% strand | P12955 |
| B | Xaa-pro dipeptidase (EC 3.4.13.9) | protein | 481 | 38% helix, 16% strand | P12955 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 810 | 0.83 | 0.86 | 82 | empty |
| 2 | 880 | 0.79 | 0.82 | 91 | empty |
| 3 | 846 | 0.78 | 0.81 | 93 | empty |
| 4 | 69 | 0.44 | 0.82 | 21 | empty |
| 5 | 112 | 0.39 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 3191 Ų buried · 44 hydrogen bonds · protein-protein
Compared structures
- 6SRF · Crystal Structure of Human Prolidase G278N variant expressed in the presence of chaperones · the same entry in another collection · chain A against A, TM-score 1.00
- P12955 · AlphaFold monomer V2.0 prediction for xaa-pro dipeptidase (P12955) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P12955
- Elsewhere: RCSB PDB 6SRF · PDBe 6SRF · UniProt P12955
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