MolNFT v1 · #15137 · protein
Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-beta-D-glucanase from fibrobacter succinogenes
1MVE · Truncated 1,3-1,4-beta-D-glucanase: “Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-beta-D-glucanase from…”. X-ray diffraction, 1 ligand (CA), 2 pockets (best druggability 0.54). MolNFT v1 #15137 on…
- PDB
- 1MVE
- Type
- protein
- Length
- 243 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Truncated 1,3-1,4-beta-D-glucanase
- EC
- 3.2.1.73
- UniProt
- P17989
- Ligands
- CA
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Truncated 1,3-1,4-beta-D-glucanase (EC 3.2.1.73) | protein | 243 | 6% helix, 49% strand | P17989 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 258 | 0.54 | 0.76 | 29 | empty |
| 2 | 52 | 0.41 | 0.82 | 20 | empty |
Modifications
Observed in the structure: 5 modified (engineered).
Compared structures
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 P17989
- Elsewhere: RCSB PDB 1MVE · PDBe 1MVE · UniProt P17989
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