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Full length bacteriophage P22 portal protein

Analyse Full length bacteriophage P22 portal protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LJ5
Type: protein
Length: 8,304 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Portal protein
UniProt: P26744
Pockets: 20 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L	Portal protein	protein	692	46% helix, 11% strand	P26744

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1022	0.84	0.85	78	empty
2	876	0.84	0.86	76	empty
3	1060	0.84	0.85	82	empty
4	1067	0.83	0.84	91	empty
5	1054	0.83	0.84	86	empty

Interfaces

24 interfaces between chains.

D–E · 5979 Å² buried · 64 hydrogen bonds · protein-protein
A–L · 5830 Å² buried · 60 hydrogen bonds · protein-protein
F–G · 5766 Å² buried · 60 hydrogen bonds · protein-protein
I–J · 5725 Å² buried · 58 hydrogen bonds · protein-protein
G–H · 5725 Å² buried · 52 hydrogen bonds · protein-protein

Compared structures

3LJ5 · Full Length Bacteriophage P22 Portal Protein · 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 P26744
Elsewhere: RCSB PDB 3LJ5 · PDBe 3LJ5 · UniProt P26744

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