MolNFT v1 · #62411 · protein
Crystal structure of a putative cobalamin biosynthesis protein G homolog from sulfolobus solfataricus
3EEQ: “Crystal structure of a putative cobalamin biosynthesis protein G homolog from sulfolobus solfataricus”. X-ray diffraction, 1 ligand (SO4), 6 pockets (best druggability 0.71). MolNFT v1 #62411 on GenesisL1: 3D structure, binding…
- PDB
- 3EEQ
- Type
- protein
- Length
- 615 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cobalamin biosynthesis protein G homolog
- UniProt
- Q97WD0
- Ligands
- SO4
- Pockets
- 6 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative cobalamin biosynthesis protein G homolog | protein | 311 | 35% helix, 26% strand | Q97WD0 |
| B | Putative cobalamin biosynthesis protein G homolog | protein | 304 | 36% helix, 27% strand | Q97WD0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 551 | 0.71 | 0.79 | 61 | empty |
| 2 | 440 | 0.69 | 0.80 | 49 | empty |
| 3 | 213 | 0.49 | 0.75 | 35 | SO4 |
| 4 | 124 | 0.45 | 0.77 | 25 | empty |
| 5 | 55 | 0.36 | 0.79 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 740 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 3EEQ · Crystal structure of a putative cobalamin biosynthesis protein G homolog from Sulfolobus… · 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 Q97WD0
- Elsewhere: RCSB PDB 3EEQ · PDBe 3EEQ · UniProt Q97WD0
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