Research workbench
Structure of CBM3B of major scaffoldin subunit scaa from acetivibrio cellulolyticus determined from the crystals grown in the presence of nickel
Analyse Structure of CBM3B of major scaffoldin subunit scaa from acetivibrio… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZUC
- Type
- protein
- Length
- 153 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellulosomal scaffoldin
- UniProt
- Q9RPL0
- Ligands
- CA, NI
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellulosomal scaffoldin | protein | 153 | 8% helix, 51% strand | Q9RPL0 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- NI · Nickel (II) ion · metal · chains A
- EDO · 1,2-ethanediol · additive · chains A
- 1PE · Pentaethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3ZUC · Structure of CBM3b of major scaffoldin subunit ScaA from Acetivibrio cellulolyticus… · 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 Q9RPL0
- Elsewhere: RCSB PDB 3ZUC · PDBe 3ZUC · UniProt Q9RPL0
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