MolNFT v1 · #146805 · protein
1.8 ångström resolution crystal structure of camp-regulatory protein from yersinia pestis in complex with camp
6DT4 · Cyclic AMP receptor protein: “1.8 ångström resolution crystal structure of camp-regulatory protein from yersinia pestis in complex with camp”. X-ray diffraction, 2 ligands (CMP, CL), 5 pockets (best druggability 0.75). MolNFT v1…
- PDB
- 6DT4
- Type
- protein
- Length
- 403 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic AMP receptor protein
- UniProt
- A0A0H2W086
- Ligands
- CMP, CL
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic AMP receptor protein | protein | 203 | 37% helix, 31% strand | A0A0H2W086 |
| B | Cyclic AMP receptor protein | protein | 200 | 38% helix, 30% strand | A0A0H2W086 |
Ligands and binding sites
- CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 3 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, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 541 | 0.75 | 0.83 | 73 | CMP |
| 2 | 127 | 0.72 | 0.92 | 26 | CMP |
| 3 | 278 | 0.54 | 0.75 | 25 | empty |
| 4 | 98 | 0.45 | 0.79 | 20 | empty |
| 5 | 64 | 0.30 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1859 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 6DT4 · 1.8 Angstrom Resolution Crystal Structure of cAMP-Regulatory Protein from Yersinia pestis… · 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 A0A0H2W086
- Elsewhere: RCSB PDB 6DT4 · PDBe 6DT4 · UniProt A0A0H2W086
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