MolNFT v1 · #88024 · protein
Structural insights into the N-terminus of the EHD2 ATPase
4CID · Eh domain-containing protein 2: “Structural insights into the N-terminus of the EHD2 ATPase”. X-ray diffraction, 3 ligands (ANP, CA, MG), 6 pockets (best druggability 0.71). MolNFT v1 #88024 on GenesisL1: 3D structure, binding sites…
- PDB
- 4CID
- Type
- protein
- Length
- 497 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eh domain-containing protein 2
- EC
- 3.6.5.5
- UniProt
- Q8BH64
- Ligands
- ANP, CA, MG
- Pockets
- 6 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eh domain-containing protein 2 (EC 3.6.5.5) | protein | 497 | 52% helix, 10% strand | Q8BH64 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- CA · Calcium ion · metal · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 390 | 0.71 | 0.83 | 40 | empty |
| 2 | 283 | 0.63 | 0.80 | 25 | empty |
| 3 | 147 | 0.58 | 0.83 | 26 | ANP, MG |
| 4 | 142 | 0.49 | 0.79 | 24 | empty |
| 5 | 129 | 0.42 | 0.76 | 27 | empty |
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 4CID · Structural insights into the N-terminus of the EHD2 ATPase · the same entry in another collection · chain A against A, TM-score 1.00
- Q8BH64 · AlphaFold monomer V2.0 prediction for eh domain-containing protein 2 (Q8BH64) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q8BH64
- Elsewhere: RCSB PDB 4CID · PDBe 4CID · UniProt Q8BH64
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