MolNFT v1 · #24405 · protein
X-ray crystal structure of the catalytic domain of humicola grisea CEL12A soaked with cellotetraose
1UU5 · Endo-beta-1,4-glucanase: “X-ray crystal structure of the catalytic domain of humicola grisea CEL12A soaked with cellotetraose”. X-ray diffraction, 1 ligand (BGC), 2 pockets (best druggability 0.54). MolNFT v1 #24405 on GenesisL1: 3D…
- PDB
- 1UU5
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-beta-1,4-glucanase
- EC
- 3.2.1.4
- UniProt
- Q8NJY3
- Ligands
- BGC
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-beta-1,4-glucanase (EC 3.2.1.4) | protein | 224 | 9% helix, 54% strand | Q8NJY3 |
Ligands and binding sites
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 | 193 | 0.54 | 0.78 | 28 | BGC |
| 2 | 51 | 0.33 | 0.78 | 17 | empty |
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 1UU5 · X-ray crystal structure of the catalytic domain of humicola grisea CEL12A soaked with… · 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 Q8NJY3
- Elsewhere: RCSB PDB 1UU5 · PDBe 1UU5 · UniProt Q8NJY3
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