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Crystal structure of clavaminate synthase with nitric oxide
Analyse Crystal structure of clavaminate synthase with nitric oxide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GVG
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clavaminate synthase 1
- EC
- 1.14.11.21
- UniProt
- Q05581
- Ligands
- AKG, PCX, HOA, FE, SO4
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Clavaminate synthase 1 (EC 1.14.11.21) | protein | 315 | 30% helix, 23% strand | Q05581 |
Ligands and binding sites
- AKG · 2-oxoglutaric acid · ligand · chains A
- PCX · Deoxyguanidinoproclavaminic acid · ligand · chains A
- HOA · Hydroxyamine · ligand · chains A
- FE · Fe (III) ion · metal · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 238 | 0.72 | 0.87 | 35 | FE, AKG, PCX, HOA |
| 2 | 61 | 0.31 | 0.75 | 14 | empty |
Compared structures
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 Q05581
- Elsewhere: RCSB PDB 1GVG · PDBe 1GVG · UniProt Q05581
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