Research workbench
Crystal structure of puud gamma-glutamyl-gamma-aminobutyrate hydrolase from E. COLI
Analyse Crystal structure of puud gamma-glutamyl-gamma-aminobutyrate hydrolase from E.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VTV
- Type
- protein
- Length
- 501 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-glutamyl-gamma-aminobutyrate hydrolase puud
- EC
- 3.5.1.94
- UniProt
- P76038
- Ligands
- MN
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma-glutamyl-gamma-aminobutyrate hydrolase puud (EC 3.5.1.94) | protein | 249 | 37% helix, 24% strand | P76038 |
| B | Gamma-glutamyl-gamma-aminobutyrate hydrolase puud (EC 3.5.1.94) | protein | 252 | 35% helix, 24% strand | P76038 |
Ligands and binding sites
- MN · Manganese (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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 323 | 0.64 | 0.80 | 44 | empty |
| 2 | 321 | 0.64 | 0.80 | 44 | empty |
| 3 | 51 | 0.43 | 0.83 | 15 | empty |
| 4 | 55 | 0.28 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1516 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 6VTV · Crystal structure of PuuD gamma-glutamyl-gamma-aminobutyrate hydrolase from E. coli · the same entry in another collection · chain A against A, TM-score 1.00
- P76038 · AlphaFold monomer V2.0 prediction for gamma-glutamyl-gamma- aminobutyrate hydrolase puud… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P76038
- Elsewhere: RCSB PDB 6VTV · PDBe 6VTV · UniProt P76038
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