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GP4D helicase from phage T7

Analyse GP4D helicase from phage T7 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1E0K
Type: protein
Length: 1,728 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA helicase
UniProt: P03692
Pockets: 20 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	DNA helicase	protein	288	31% helix, 18% strand	P03692

Pockets

20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	969	0.83	0.84	95	empty
2	1182	0.80	0.81	98	empty
3	954	0.80	0.82	84	empty
4	1159	0.80	0.81	101	empty
5	213	0.54	0.78	33	empty

Interfaces

5 interfaces between chains.

E–F · 2033 Å² buried · 27 hydrogen bonds · protein-protein
B–C · 1997 Å² buried · 34 hydrogen bonds · protein-protein
A–B · 1876 Å² buried · 21 hydrogen bonds · protein-protein
D–E · 1851 Å² buried · 28 hydrogen bonds · protein-protein
B–E · 28 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1E0K · gp4d helicase from phage T7 · 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 P03692
Elsewhere: RCSB PDB 1E0K · PDBe 1E0K · UniProt P03692

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