MolNFT v1 · #164677 · protein
Ecv-1 from echinicola vietnamensis. environmental metallo-beta- lactamases exhibit high enzymatic activity under zinc deprivation
6T5K · Zn-dependent hydrolase, glyoxylase: “Ecv-1 from echinicola vietnamensis. environmental metallo-beta- lactamases exhibit high enzymatic activity…”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.49). MolNFT v1…
- PDB
- 6T5K
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Zn-dependent hydrolase, glyoxylase
- UniProt
- L0FY79
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Zn-dependent hydrolase, glyoxylase | protein | 224 | 25% helix, 34% strand | L0FY79 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 188 | 0.49 | 0.76 | 29 | ZN |
Compared structures
- 6T5K · ECV-1 from Echinicola vietnamensis. Environmental metallo-beta-lactamases exhibit high… · the same entry in another collection · chain C against C, 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 L0FY79
- Elsewhere: RCSB PDB 6T5K · PDBe 6T5K · UniProt L0FY79
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