Research workbench
Peptide-binding domain of heat shock 70 kda protein D precursor from C.ELEGANS
Analyse Peptide-binding domain of heat shock 70 kda protein D precursor from C.ELEGANS in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OP6
- Type
- protein
- Length
- 150 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock 70 kda protein D
- UniProt
- P20163
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock 70 kda protein D | protein | 150 | 17% helix, 40% strand | P20163 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.51 | 0.80 | 19 | empty |
| 2 | 112 | 0.40 | 0.75 | 17 | empty |
Compared structures
- 2OP6 · Peptide-binding domain of Heat shock 70 kDa protein D precursor from C.elegans · the same entry in another collection · chain A against A, TM-score 1.00
- P20163 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum chaperone bip homolog (P20163) · a predicted model of the same protein · chain A against A, TM-score 0.71
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 P20163
- Elsewhere: RCSB PDB 2OP6 · PDBe 2OP6 · UniProt P20163
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