Research workbench
Crystal structure of a chpt protein (CC_3470) from caulobacter crescentus CB15 at 2.30 a resolution
Analyse Crystal structure of a chpt protein (CC_3470) from caulobacter crescentus CB15… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FMT
- Type
- protein
- Length
- 833 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chpt protein
- UniProt
- Q9A2T6
- Ligands
- NA
- Pockets
- 7 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chpt protein | protein | 209 | 52% helix, 20% strand | Q9A2T6 |
| B, C, D | Chpt protein | protein | 208 | 52% helix, 20% strand | Q9A2T6 |
Ligands and binding sites
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D
- GOL · Glycerol · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 752 | 0.69 | 0.76 | 80 | NA |
| 2 | 217 | 0.51 | 0.76 | 35 | empty |
| 3 | 163 | 0.51 | 0.79 | 25 | empty |
| 4 | 210 | 0.51 | 0.76 | 39 | empty |
| 5 | 195 | 0.49 | 0.76 | 28 | empty |
Interfaces
4 interfaces between chains.
- A–B · 1471 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 1442 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 353 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 151 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4FMT · Crystal structure of a ChpT protein (CC_3470) from Caulobacter crescentus CB15 at 2.30 A… · 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 Q9A2T6
- Elsewhere: RCSB PDB 4FMT · PDBe 4FMT · UniProt Q9A2T6
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