Research workbench
NMR structure and calcium-binding properties of the tellurite resistance protein terd from klebsiella pneumoniae
Analyse NMR structure and calcium-binding properties of the tellurite resistance… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2KXV
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tellurite resistance protein
- UniProt
- C4XDJ3
- Ligands
- CA
- Pockets
- 1 · best druggability 0.25
Structure
solution nmr · 1 distinct chain · 13% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tellurite resistance protein | protein | 174 | 13% helix, 34% strand | C4XDJ3 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.25 | 0.73 | 14 | empty |
Compared structures
- 2KXV · NMR structure and calcium-binding properties of the tellurite resistance protein TerD… · 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 C4XDJ3
- Elsewhere: RCSB PDB 2KXV · PDBe 2KXV · UniProt C4XDJ3
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