Research workbench
Mutm interrogating an extrahelical G
Analyse Mutm interrogating an extrahelical G in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3JR4
- Type
- protein + DNA
- Length
- 285 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA glycosylase; DNA (5'-D(*AP*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)- 3'); DNA…
- EC
- 4.2.99.18
- UniProt
- P84131
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 3 distinct chains · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA glycosylase (EC 4.2.99.18) | protein | 263 | 31% helix, 25% strand | P84131 |
| B | DNA (5'-D(*AP*GP*GP*TP*AP*GP*AP*CP*CP*TP*GP*GP*AP*CP*GP*C)- 3') | dna | 11 | — | — |
| C | DNA (5'-D(*TP*G*CP*GP*TP*CP*CP*AP*(GX1) P*GP*TP*CP*TP*AP*CP*C)-3') | dna | 11 | — | — |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 543 | 0.65 | 0.77 | 43 | empty |
| 2 | 113 | 0.35 | 0.73 | 20 | empty |
| 3 | 92 | 0.31 | 0.73 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–C · 722 Ų buried · 12 hydrogen bonds · protein-nucleic
- B–C · 472 Ų buried · 44 hydrogen bonds · nucleic-nucleic
- A–B · 346 Ų buried · 7 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 3JR4 · MutM interrogating an extrahelical G · 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 P84131
- Elsewhere: RCSB PDB 3JR4 · PDBe 3JR4 · UniProt P84131
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