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Crystal structure of cysteine desulfurase from elizabethkingia anophelis with covalently bound pyridoxal phosphate
Analyse Crystal structure of cysteine desulfurase from elizabethkingia anophelis with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VPR
- Type
- protein
- Length
- 366 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cysteine desulfurase
- EC
- 2.8.1.7
- UniProt
- A0A077EMQ8
- Pockets
- 2 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine desulfurase (EC 2.8.1.7) | protein | 366 | 46% helix, 17% strand | A0A077EMQ8 |
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 | 181 | 0.55 | 0.79 | 24 | empty |
| 2 | 54 | 0.31 | 0.77 | 15 | empty |
Modifications
Observed in the structure: 1 modified (cofactor).
Compared structures
- 5VPR · Crystal Structure of Cysteine desulfurase from Elizabethkingia anophelis with covalently… · 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 A0A077EMQ8
- Elsewhere: RCSB PDB 5VPR · PDBe 5VPR · UniProt A0A077EMQ8
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