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Structure and mutation analysis of the hexameric P4 from pseudomonas aeruginosa phage phiyy

Analyse Structure and mutation analysis of the hexameric P4 from pseudomonas aeruginosa… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ESO
Type: protein
Length: 2,092 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Packaging NTPase
UniProt: A0A1U9AK63
Pockets: 20 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, H, C, E	Packaging NTPase	protein	266	36% helix, 22% strand	A0A1U9AK63
B, G, D, F	Packaging NTPase	protein	257	35% helix, 21% strand	A0A1U9AK63

Pockets

20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	958	0.78	0.80	117	empty
2	621	0.73	0.80	52	empty
3	603	0.71	0.79	63	empty
4	659	0.70	0.78	65	empty
5	469	0.70	0.80	63	empty

Interfaces

8 interfaces between chains.

B–C · 1551 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1517 Å² buried · 18 hydrogen bonds · protein-protein
A–F · 1516 Å² buried · 16 hydrogen bonds · protein-protein
D–E · 1515 Å² buried · 20 hydrogen bonds · protein-protein
E–F · 1514 Å² buried · 15 hydrogen bonds · protein-protein

Analyse

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Every structure of UniProt A0A1U9AK63
Elsewhere: RCSB PDB 7ESO · PDBe 7ESO · UniProt A0A1U9AK63

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