Research workbench
T4 phage bgt in complex with udp and MN2+
Analyse T4 phage bgt in complex with udp and MN2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JG7
- Type
- protein
- Length
- 351 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA beta-glucosyltransferase
- EC
- 2.4.1.27
- UniProt
- P04547
- Ligands
- UDP, MN
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA beta-glucosyltransferase (EC 2.4.1.27) | protein | 351 | 39% helix, 17% strand | P04547 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 474 | 0.76 | 0.85 | 46 | MN, UDP |
| 2 | 141 | 0.45 | 0.76 | 27 | empty |
| 3 | 102 | 0.44 | 0.79 | 17 | empty |
Compared structures
- 1JG7 · T4 phage BGT in complex with UDP and Mn2+ · 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 P04547
- Elsewhere: RCSB PDB 1JG7 · PDBe 1JG7 · UniProt P04547
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