Research workbench
Crystal structure of the pectin methylesterase from aspergillus niger in deglycosylated form
Analyse Crystal structure of the pectin methylesterase from aspergillus niger in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5C1C
- Type
- protein
- Length
- 299 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pectinesterase
- EC
- 3.1.1.11
- UniProt
- G3YAL0
- Ligands
- SO4, CL
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pectinesterase (EC 3.1.1.11) | protein | 299 | 8% helix, 37% strand | G3YAL0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A
- CL · Chloride ion · ion · chains A
- GOL · Glycerol · additive · 3 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5C1C · Crystal Structure of the Pectin Methylesterase from Aspergillus niger in Deglycosylated… · 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 G3YAL0
- Elsewhere: RCSB PDB 5C1C · PDBe 5C1C · UniProt G3YAL0
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