MolNFT v1 · #90825 · protein
Crystal structure of thermus thermophilus catabolite activator protein
4EV0 · Transcription regulator, crp family: “Crystal structure of thermus thermophilus catabolite activator protein”. X-ray diffraction, 3 ligands (CMP, MG, SO4), 4 pockets (best druggability 0.70). MolNFT v1 #90825 on GenesisL1: 3D…
- PDB
- 4EV0
- Type
- protein
- Length
- 427 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transcription regulator, crp family
- UniProt
- Q5SID7
- Ligands
- CMP, MG, SO4
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transcription regulator, crp family | protein | 213 | 46% helix, 25% strand | Q5SID7 |
| D | Transcription regulator, crp family | protein | 214 | 44% helix, 25% strand | Q5SID7 |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains A, D
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · 5 copies · chains A, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 621 | 0.70 | 0.78 | 62 | CMP |
| 2 | 208 | 0.66 | 0.84 | 29 | CMP |
| 3 | 78 | 0.40 | 0.79 | 16 | empty |
| 4 | 73 | 0.31 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–D · 2439 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 4EV0 · Crystal Structure of Thermus thermophilus Catabolite Activator Protein · the same entry in another collection · chain A against A, TM-score 1.00
- Q5SID7 · AlphaFold monomer V2.0 prediction for cyclic AMP receptor protein (Q5SID7) · a predicted model of the same protein · chain D against A, TM-score 0.64
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 Q5SID7
- Elsewhere: RCSB PDB 4EV0 · PDBe 4EV0 · UniProt Q5SID7
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