MolNFT v1 · #173453 · protein
Sugar transaminase from archaeoglobus veneficus
7B0D · Glutamine--scyllo-inositol transaminase: “Sugar transaminase from archaeoglobus veneficus”. X-ray diffraction, 2 ligands (CA, PO4), 3 pockets (best druggability 0.75). MolNFT v1 #173453 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7B0D
- Type
- protein
- Length
- 736 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutamine--scyllo-inositol transaminase
- EC
- 2.6.1.50
- UniProt
- F2KQE6
- Ligands
- CA, PO4
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Glutamine--scyllo-inositol transaminase (EC 2.6.1.50) | protein | 368 | 42% helix, 16% strand | F2KQE6 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A, B
- PO4 · Phosphate ion · ion · 10 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 14 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 511 | 0.75 | 0.83 | 50 | EDO, PO4 |
| 2 | 515 | 0.72 | 0.81 | 45 | EDO, PO4 |
| 3 | 188 | 0.44 | 0.74 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 2386 Ų buried · 36 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 2 modified (disulfide, cofactor).
Compared structures
- 7B0D · Sugar transaminase from Archaeoglobus veneficus · 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 F2KQE6
- Elsewhere: RCSB PDB 7B0D · PDBe 7B0D · UniProt F2KQE6
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