MolNFT v1 · #22394 · protein
Crystal structure of the E.COLI dnag C-terminal domain (residues 434 to 581)
1T3W · DNA primase: “Crystal structure of the E.COLI dnag C-terminal domain (residues 434 to 581)”. X-ray diffraction, 1 pocket (best druggability 0.37). MolNFT v1 #22394 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1T3W
- Type
- protein
- Length
- 269 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA primase
- EC
- 2.7.7.-
- UniProt
- P0ABS5
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA primase (EC 2.7.7.-) | protein | 134 | 74% helix, 0% strand | P0ABS5 |
| B | DNA primase (EC 2.7.7.-) | protein | 135 | 64% helix, 0% strand | P0ABS5 |
Ligands and binding sites
- ACY · Acetic acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 74 | 0.37 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1579 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
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 P0ABS5
- Elsewhere: RCSB PDB 1T3W · PDBe 1T3W · UniProt P0ABS5
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