MolNFT v1 · #85922 · protein

Dodecahedron formed of penton base protein from adenovirus AD3

4AR2 · L2 protein III (penton base): “Dodecahedron formed of penton base protein from adenovirus AD3”. X-ray diffraction, 1 ligand (CA), 4 pockets (best druggability 0.44). MolNFT v1 #85922 on GenesisL1: 3D structure, binding sites and…

PDB: 4AR2
Type: protein
Length: 465 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: L2 protein III (penton base); Fiber protein
UniProt: Q2Y0H9, P03275
Ligands: CA
Pockets: 4 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 13% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	L2 protein III (penton base)	protein	455	14% helix, 25% strand	Q2Y0H9
P	Fiber protein	protein	10	0% helix, 0% strand	P03275

Ligands and binding sites

CA · Calcium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	143	0.44	0.76	21	empty
2	155	0.40	0.73	21	empty
3	51	0.39	0.81	21	empty
4	99	0.34	0.73	18	empty

Interfaces

1 interface between chains.

A–P · 485 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4AR2 · Dodecahedron formed of penton base protein from adenovirus Ad3 · 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 Q2Y0H9
Every structure of UniProt P03275
Elsewhere: RCSB PDB 4AR2 · PDBe 4AR2 · UniProt Q2Y0H9 · UniProt P03275

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