Research workbench
Crystal structure of imazg from vibrio dat 722: ctag-imazg (P43212)
Analyse Crystal structure of imazg from vibrio dat 722: ctag-imazg (P43212) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q9L
- Type
- protein
- Length
- 337 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- EC
- 3.6.1.19
- UniProt
- Q2F9Z1
- Ligands
- MG
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 3 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Hypothetical protein (EC 3.6.1.19) | protein | 90 | 76% helix, 1% strand | Q2F9Z1 |
| C | Hypothetical protein (EC 3.6.1.19) | protein | 79 | 73% helix, 0% strand | Q2F9Z1 |
| D | Hypothetical protein (EC 3.6.1.19) | protein | 78 | 74% helix, 0% strand | Q2F9Z1 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 98 | 0.38 | 0.75 | 16 | empty |
| 2 | 62 | 0.30 | 0.75 | 13 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1992 Ų buried · 18 hydrogen bonds · protein-protein
- C–D · 1676 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 529 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 517 Ų buried · 7 hydrogen bonds · protein-protein
- A–D · 224 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2Q9L · Crystal structure of iMazG from Vibrio DAT 722: Ctag-iMazG (P43212) · 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 Q2F9Z1
- Elsewhere: RCSB PDB 2Q9L · PDBe 2Q9L · UniProt Q2F9Z1
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