Research workbench
The structure of spirochaeta thermophila CBM64
Analyse The structure of spirochaeta thermophila CBM64 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LU3
- Type
- protein
- Length
- 88 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoside hydrolase family 12
- UniProt
- G0GE26
- Ligands
- 2NV, SSN, CA, NI
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoside hydrolase family 12 | protein | 88 | 3% helix, 48% strand | G0GE26 |
Ligands and binding sites
- 2NV · 3,6,9,12,15-pentaoxaoctadecan-17-amine · ligand · chains A
- SSN · 4-oxobutanoic acid · ligand · chains A
- CA · Calcium ion · metal · chains A
- NI · Nickel (II) ion · metal · chains A
- FMT · Formic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5LU3 · The Structure of Spirochaeta thermophila CBM64 · 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 G0GE26
- Elsewhere: RCSB PDB 5LU3 · PDBe 5LU3 · UniProt G0GE26
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