Research workbench
Structure of C. glabrata HRR25 bound to ADP (SO4 condition)
Analyse Structure of C. glabrata HRR25 bound to ADP (SO4 condition) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XH0
- Type
- protein
- Length
- 350 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Similar to UNIPROT|P29295 saccharomyces cerevisiae YPL204W HRR25
- EC
- 2.7.11.1
- UniProt
- Q6FS46
- Ligands
- ADP, SO4
- Pockets
- 2 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Similar to UNIPROT|P29295 saccharomyces cerevisiae YPL204W HRR25 (EC 2.7.11.1) | protein | 350 | 45% helix, 15% strand | Q6FS46 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.48 | 0.79 | 21 | ADP |
| 2 | 50 | 0.27 | 0.75 | 14 | empty |
Compared structures
- 4XH0 · Structure of C. glabrata Hrr25 bound to ADP (SO4 condition) · 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 Q6FS46
- Elsewhere: RCSB PDB 4XH0 · PDBe 4XH0 · UniProt Q6FS46
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