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Structure of the distal domain of mouse adenovirus 2 fibre, P212121 native

Analyse Structure of the distal domain of mouse adenovirus 2 fibre, P212121 native in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5NBH
Type: protein
Length: 582 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fiber
UniProt: E7CH51
Pockets: 5 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Fiber	protein	194	2% helix, 55% strand	E7CH51

Ligands and binding sites

GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	207	0.84	0.97	29	empty
2	222	0.61	0.81	40	empty
3	214	0.60	0.81	40	empty
4	217	0.59	0.81	29	empty
5	61	0.32	0.76	14	empty

Interfaces

3 interfaces between chains.

A–B · 1967 Å² buried · 19 hydrogen bonds · protein-protein
B–C · 1907 Å² buried · 21 hydrogen bonds · protein-protein
A–C · 1898 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

5NBH · Structure of the distal domain of mouse adenovirus 2 fibre, P212121 native · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt E7CH51
Elsewhere: RCSB PDB 5NBH · PDBe 5NBH · UniProt E7CH51

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