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Extended E2 DNA-binding domain of the bovine papillomavirus-1

Analyse Extended E2 DNA-binding domain of the bovine papillomavirus-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6BUS
Type: protein
Length: 371 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Regulatory protein E2
UniProt: P03122
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
1, 2, 4	Regulatory protein E2	protein	92	29% helix, 37% strand	P03122
3	Regulatory protein E2	protein	95	28% helix, 28% strand	P03122

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	336	0.63	0.78	28	empty
2	251	0.60	0.80	27	empty
3	301	0.59	0.77	29	empty
4	191	0.56	0.79	22	empty

Interfaces

4 interfaces between chains.

1–2 · 1425 Å² buried · 39 hydrogen bonds · protein-protein
3–4 · 1329 Å² buried · 35 hydrogen bonds · protein-protein
1–4 · 215 Å² buried · 2 hydrogen bonds · protein-protein
1–3 · 75 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6BUS · Extended E2 DNA-binding domain of the Bovine Papillomavirus-1 · the same entry in another collection · chain 1 against 1, 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 P03122
Elsewhere: RCSB PDB 6BUS · PDBe 6BUS · UniProt P03122

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