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Structure of an allelic variant of puccinia graminis F. sp. tritici (pgt) effector AVRSR50 (qcmjc)
Analyse Structure of an allelic variant of puccinia graminis F. sp. tritici (pgt)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7MQQ
- Type
- protein
- Length
- 113 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Stem rust effector protein AVRSR50
- UniProt
- A0A5B0MRS6
- Ligands
- MG
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Stem rust effector protein AVRSR50 | protein | 113 | 9% helix, 37% strand | A0A5B0MRS6 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.27 | 0.73 | 12 | empty |
Compared structures
- 7MQQ · Structure of an allelic variant of Puccinia graminis f. sp. tritici (Pgt) effector… · 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 A0A5B0MRS6
- Elsewhere: RCSB PDB 7MQQ · PDBe 7MQQ · UniProt A0A5B0MRS6
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