Research workbench
Mutm slanted complex 4 with R112A mutation
Analyse Mutm slanted complex 4 with R112A mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3SAS
- Type
- protein + DNA
- Length
- 282 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA glycosylase; 5'-D(*A*GP*GP*TP*AP*GP*AP*CP*TP*CP*GP*GP*AP*CP*GP*C)-3'…
- EC
- 4.2.99.18
- UniProt
- P84131
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 3 distinct chains · 32% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA glycosylase (EC 4.2.99.18) | protein | 253 | 32% helix, 26% strand | P84131 |
| B | 5'-D(*A*GP*GP*TP*AP*GP*AP*CP*TP*CP*GP*GP*AP*CP*GP*C)-3' | dna | 15 | — | — |
| C | 5'-D(*T*GP*CP*GP*TP*CP*CP*GP*AP*GP*(TX2) P*CP*TP*AP*CP*C)- 3' | dna | 14 | — | — |
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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 522 | 0.67 | 0.78 | 44 | empty |
| 2 | 127 | 0.50 | 0.80 | 17 | empty |
Interfaces
3 interfaces between chains.
- B–C · 649 Ų buried · 70 hydrogen bonds · nucleic-nucleic
- A–C · 551 Ų buried · 8 hydrogen bonds · protein-nucleic
- A–B · 386 Ų buried · 7 hydrogen bonds · protein-nucleic
Modifications
Observed in the structure: 1 modified (nucleotide modification).
Compared structures
- 3SAS · MUTM Slanted complex 4 with R112A mutation · 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 3SAS · PDBe 3SAS · UniProt P84131
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