Research workbench
Crystal structure of a sub-domain of the nucleotidyltransferase (adenylation) domain of human DNA ligase IV
Analyse Crystal structure of a sub-domain of the nucleotidyltransferase (adenylation)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VNN
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA ligase 4
- EC
- 6.5.1.1
- UniProt
- P49917
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA ligase 4 (EC 6.5.1.1) | protein | 124 | 11% helix, 36% strand | P49917 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.40 | 0.79 | 15 | empty |
Compared structures
- 3VNN · Crystal Structure of a sub-domain of the nucleotidyltransferase (adenylation) domain of… · the same entry in another collection · chain A against A, TM-score 1.00
- P49917 · AlphaFold monomer V2.0 prediction for DNA ligase 4 (P49917) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 P49917
- Elsewhere: RCSB PDB 3VNN · PDBe 3VNN · UniProt P49917
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