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Crystal structure of the N-terminal domain of HSP70 (CGD2_20) from cryptosporidium parvum in complex with amppnp
Analyse Crystal structure of the N-terminal domain of HSP70 (CGD2_20) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KVG
- Type
- protein
- Length
- 763 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock 70 (HSP70) protein
- UniProt
- Q5CPP8
- Ligands
- ANP, PO4
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heat shock 70 (HSP70) protein | protein | 381 | 40% helix, 28% strand | Q5CPP8 |
| B | Heat shock 70 (HSP70) protein | protein | 382 | 40% helix, 28% strand | Q5CPP8 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · chains A, B
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 695 | 0.79 | 0.84 | 72 | EDO |
| 2 | 258 | 0.78 | 0.91 | 45 | ANP |
| 3 | 211 | 0.74 | 0.90 | 36 | ANP |
| 4 | 456 | 0.63 | 0.77 | 45 | EDO |
| 5 | 290 | 0.58 | 0.78 | 26 | EDO |
Interfaces
1 interface between chains.
- A–B · 989 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 3KVG · Crystal structure of the N-terminal domain of Hsp70 (cgd2_20) from Cryptosporidium parvum… · the same entry in another collection · 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 Q5CPP8
- Elsewhere: RCSB PDB 3KVG · PDBe 3KVG · UniProt Q5CPP8
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