Research workbench
Structure of RV1264N, the regulatory domain of the mycobacterial adenylyl cylcase RV1264, at pH 6.0
Analyse Structure of RV1264N, the regulatory domain of the mycobacterial adenylyl… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EV1
- Type
- protein
- Length
- 366 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein RV1264/MT1302
- EC
- 4.6.1.1
- UniProt
- Q11055
- Ligands
- OLA
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 70% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hypothetical protein RV1264/MT1302 (EC 4.6.1.1) | protein | 185 | 70% helix, 2% strand | Q11055 |
| B | Hypothetical protein RV1264/MT1302 (EC 4.6.1.1) | protein | 181 | 70% helix, 2% strand | Q11055 |
Ligands and binding sites
- OLA · Oleic acid · ligand · 2 copies · chains A, B
- 1PE · Pentaethylene glycol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 345 | 0.82 | 0.91 | 58 | OLA |
| 2 | 299 | 0.79 | 0.89 | 48 | OLA |
| 3 | 69 | 0.47 | 0.83 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 3235 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 2EV1 · Structure of Rv1264N, the regulatory domain of the mycobacterial adenylyl cylcase Rv1264… · 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 Q11055
- Elsewhere: RCSB PDB 2EV1 · PDBe 2EV1 · UniProt Q11055
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