Research workbench
Crystal structure of the effector binding domain of a catm variant, CATM(V158M)
Analyse Crystal structure of the effector binding domain of a catm variant, CATM(V158M) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H98
- Type
- protein
- Length
- 432 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hth-type transcriptional regulator catm
- UniProt
- P07774
- Ligands
- CL
- Pockets
- 5 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hth-type transcriptional regulator catm | protein | 216 | 35% helix, 27% strand | P07774 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.68 | 0.83 | 34 | empty |
| 2 | 161 | 0.59 | 0.82 | 39 | empty |
| 3 | 121 | 0.57 | 0.84 | 22 | empty |
| 4 | 96 | 0.57 | 0.86 | 28 | CL |
| 5 | 51 | 0.28 | 0.74 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 1462 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 2H98 · Crystal structure of the effector binding domain of a CatM variant, CatM(V158M) · the same entry in another collection · chain A against A, TM-score 1.00
- P07774 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator catm (P07774) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P07774
- Elsewhere: RCSB PDB 2H98 · PDBe 2H98 · UniProt P07774
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