Research workbench
Human DNA polymerase eta R61A-DNA ternary complex: reaction with 1 mm MG2+ for 140S
Analyse Human DNA polymerase eta R61A-DNA ternary complex: reaction with 1 mm MG2+ for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KFV
- Type
- protein + DNA
- Length
- 449 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9Y253
- Ligands
- DTP, MG, CA, K
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 430 | — | Q9Y253 |
| T | — | dna | 11 | — | — |
| P | — | dna | 8 | — | — |
Ligands and binding sites
- DTP · 2'-deoxyadenosine 5'-triphosphate · ligand · chains A, T, P
- MG · Magnesium ion · metal · 2 copies · chains A, P
- CA · Calcium ion · metal · chains A
- K · Potassium ion · metal · chains A, P
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5KFV · Human DNA polymerase eta R61A-DNA ternary complex: reaction with 1 mM Mg2+ for 140s · 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 Q9Y253
- Elsewhere: RCSB PDB 5KFV · PDBe 5KFV · UniProt Q9Y253
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