Research workbench
Proton relay pathway in inverting cellulase
Analyse Proton relay pathway in inverting cellulase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3X2N
- Type
- protein
- Length
- 180 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase V-like protein
- UniProt
- B3Y002
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase V-like protein | protein | 180 | 13% helix, 27% strand | B3Y002 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 3X2N · Proton relay pathway in inverting cellulase · 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 B3Y002
- Elsewhere: RCSB PDB 3X2N · PDBe 3X2N · UniProt B3Y002
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