Research workbench
Crystal structure of crp (camp receptor protein) from mycobacterium tuberculosis
Analyse Crystal structure of crp (camp receptor protein) from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H3U
- Type
- protein
- Length
- 430 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable transcriptional regulatory protein (probably CRP/FNR-family)
- UniProt
- O69644
- Ligands
- CMP, SO4
- Pockets
- 7 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable transcriptional regulatory protein (probably CRP/FNR-family) | protein | 216 | 43% helix, 28% strand | O69644 |
| B | Probable transcriptional regulatory protein (probably CRP/FNR-family) | protein | 214 | 43% helix, 27% strand | O69644 |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · chains B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 539 | 0.80 | 0.86 | 55 | SO4 |
| 2 | 513 | 0.78 | 0.85 | 43 | SO4 |
| 3 | 633 | 0.78 | 0.83 | 51 | empty |
| 4 | 172 | 0.56 | 0.80 | 22 | empty |
| 5 | 94 | 0.50 | 0.82 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1942 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 3H3U · Crystal structure of CRP (cAMP receptor Protein) from Mycobacterium tuberculosis · 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 O69644
- Elsewhere: RCSB PDB 3H3U · PDBe 3H3U · UniProt O69644
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