Research workbench
Crystal structure of an inactivated npu siclopps intein with cfahpq extein
Analyse Crystal structure of an inactivated npu siclopps intein with cfahpq extein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OL7
- Type
- protein
- Length
- 143 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA-directed DNA POLYMERASE,DNA-directed DNA polymerase
- EC
- 2.7.7.7
- UniProt
- B2J821, B2J066
- Ligands
- CA, CO
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed DNA POLYMERASE,DNA-directed DNA polymerase (EC 2.7.7.7) | protein | 143 | 10% helix, 55% strand | B2J821, B2J066 |
Ligands and binding sites
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 | 63 | 0.42 | 0.81 | 12 | empty |
Compared structures
- 5OL7 · Crystal structure of an inactivated Npu SICLOPPS intein with CFAHPQ extein · 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 B2J821
- Every structure of UniProt B2J066
- Elsewhere: RCSB PDB 5OL7 · PDBe 5OL7 · UniProt B2J821 · UniProt B2J066
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