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Structure of XOO1075, a peptide deformyase from xanthomonas oryzae pv. oryze, in complex with fragment 493
Analyse Structure of XOO1075, a peptide deformyase from xanthomonas oryzae pv. oryze… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5CVK
- Type
- protein
- Length
- 169 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptide deformylase
- EC
- 3.5.1.88
- UniProt
- Q5H3Z2
- Ligands
- 56E, CD, NA
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptide deformylase (EC 3.5.1.88) | protein | 169 | 26% helix, 34% strand | Q5H3Z2 |
Ligands and binding sites
- 56E · ethyl N-[(5-methylthiophen-3-yl)carbonyl]glycinate · ligand · chains A
- CD · Cadmium ion · metal · 5 copies · chains A
- NA · Sodium ion · metal · chains A
- ACT · Acetate ion · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 217 | 0.55 | 0.78 | 41 | 56E, CD |
Compared structures
- 5CVK · Structure of Xoo1075, a peptide deformyase from Xanthomonas oryzae pv. oryze, in complex… · 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 Q5H3Z2
- Elsewhere: RCSB PDB 5CVK · PDBe 5CVK · UniProt Q5H3Z2
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