MolNFT v1 · #150298 · protein
Crystal structure of the csid glutarate hydroxylase
6GPE · Protein csid: “Crystal structure of the csid glutarate hydroxylase”. X-ray diffraction, 1 ligand (FE2), 4 pockets (best druggability 0.68). MolNFT v1 #150298 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6GPE
- Type
- protein
- Length
- 583 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein csid
- UniProt
- P76621
- Ligands
- FE2
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein csid | protein | 291 | 29% helix, 30% strand | P76621 |
| B | Protein csid | protein | 292 | 28% helix, 30% strand | P76621 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 423 | 0.68 | 0.80 | 48 | FE2 |
| 2 | 404 | 0.66 | 0.79 | 45 | FE2 |
| 3 | 333 | 0.56 | 0.75 | 42 | empty |
| 4 | 152 | 0.40 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 697 Ų buried · 12 hydrogen bonds · protein-protein
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 P76621
- Elsewhere: RCSB PDB 6GPE · PDBe 6GPE · UniProt P76621
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