Research workbench
The structure of CBM51 from clostridium perfringens GH95
Analyse The structure of CBM51 from clostridium perfringens GH95 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VMH
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibronectin type III domain protein
- UniProt
- Q0TP83
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibronectin type III domain protein | protein | 147 | 4% helix, 48% strand | Q0TP83 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2VMH · The structure of CBM51 from Clostridium perfringens GH95 · 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 Q0TP83
- Elsewhere: RCSB PDB 2VMH · PDBe 2VMH · UniProt Q0TP83
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