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Crystal structure of T7 bacteriophage portal protein, 13MER, closed valve

Analyse Crystal structure of T7 bacteriophage portal protein, 13MER, closed valve in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6QWP
Type: protein
Length: 6,318 residues
Chains: 13
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Portal protein
UniProt: P03728
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M	Portal protein	protein	486	50% helix, 14% strand	P03728

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	894	0.86	0.88	107	empty
2	1036	0.85	0.86	107	empty
3	1061	0.85	0.86	106	empty
4	1027	0.85	0.86	101	empty
5	1011	0.85	0.86	112	empty

Interfaces

26 interfaces between chains.

F–G · 5291 Å² buried · 50 hydrogen bonds · protein-protein
A–M · 5270 Å² buried · 54 hydrogen bonds · protein-protein
K–L · 5266 Å² buried · 49 hydrogen bonds · protein-protein
D–E · 5262 Å² buried · 46 hydrogen bonds · protein-protein
E–F · 5260 Å² buried · 53 hydrogen bonds · protein-protein

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 P03728
Elsewhere: RCSB PDB 6QWP · PDBe 6QWP · UniProt P03728

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