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The structure of bacteriophage PHI29 scaffolding protein GP7 after prohead assembly

Analyse The structure of bacteriophage PHI29 scaffolding protein GP7 after prohead… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NOH
Type: protein
Length: 292 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Head morphogenesis protein
UniProt: P13848
Pockets: 1 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Head morphogenesis protein	protein	73	85% helix, 0% strand	P13848

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	101	0.41	0.77	14	empty

Interfaces

5 interfaces between chains.

C–D · 1975 Å² buried · 23 hydrogen bonds · protein-protein
A–B · 1958 Å² buried · 25 hydrogen bonds · protein-protein
A–D · 439 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 294 Å² buried · 2 hydrogen bonds · protein-protein
B–C · 145 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

1NOH · The structure of bacteriophage phi29 scaffolding protein gp7 after prohead assembly · the same entry in another collection · chain D against D, 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 P13848
Elsewhere: RCSB PDB 1NOH · PDBe 1NOH · UniProt P13848

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