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Structure of the bacteriophage C1 tail knob protein, GP12

Analyse Structure of the bacteriophage C1 tail knob protein, GP12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4EO2
Type: protein
Length: 2,928 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Major tail protein
UniProt: Q7Y3F0
Pockets: 20 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Major tail protein	protein	488	21% helix, 30% strand	Q7Y3F0

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	430	0.70	0.81	58	empty
2	428	0.69	0.81	61	empty
3	412	0.69	0.81	52	empty
4	439	0.69	0.80	56	empty
5	459	0.69	0.80	60	empty

Interfaces

6 interfaces between chains.

D–E · 2809 Å² buried · 34 hydrogen bonds · protein-protein
A–B · 2808 Å² buried · 33 hydrogen bonds · protein-protein
A–F · 2806 Å² buried · 32 hydrogen bonds · protein-protein
C–D · 2781 Å² buried · 29 hydrogen bonds · protein-protein
B–C · 2759 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

4EO2 · Structure of the bacteriophage C1 tail knob protein, gp12 · 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 Q7Y3F0
Elsewhere: RCSB PDB 4EO2 · PDBe 4EO2 · UniProt Q7Y3F0

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