MolNFT v1 · #49045 · protein
Crystal structure of the protein-disulfide isomerase related chaperone ERP29
2QC7 · Endoplasmic reticulum protein ERP29: “Crystal structure of the protein-disulfide isomerase related chaperone ERP29”. X-ray diffraction, 7 pockets (best druggability 0.57). MolNFT v1 #49045 on GenesisL1: 3D structure, binding sites…
- PDB
- 2QC7
- Type
- protein
- Length
- 448 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoplasmic reticulum protein ERP29
- UniProt
- P30040
- Pockets
- 7 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 50% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Endoplasmic reticulum protein ERP29 | protein | 224 | 50% helix, 10% strand | P30040 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 367 | 0.57 | 0.75 | 49 | empty |
| 2 | 86 | 0.41 | 0.78 | 20 | empty |
| 3 | 79 | 0.38 | 0.77 | 20 | empty |
| 4 | 85 | 0.35 | 0.75 | 21 | empty |
| 5 | 84 | 0.34 | 0.75 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 183 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2QC7 · Crystal structure of the protein-disulfide isomerase related chaperone ERp29 · the same entry in another collection · chain A against A, TM-score 1.00
- P30040 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum resident protein 29 (P30040) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P30040
- Elsewhere: RCSB PDB 2QC7 · PDBe 2QC7 · UniProt P30040
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