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Human adenovirus penton base 2 12 chimera

Analyse Human adenovirus penton base 2 12 chimera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2C6S
Type: protein
Length: 6,645 residues
Chains: 15
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenovirus 2,12 penton base chimera
UniProt: P03276
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O	Adenovirus 2,12 penton base chimera	protein	443	13% helix, 27% strand	P03276

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	707	0.82	0.85	45	empty
2	550	0.81	0.87	45	empty
3	890	0.81	0.83	56	empty
4	630	0.81	0.85	45	empty
5	579	0.80	0.85	42	empty

Interfaces

23 interfaces between chains.

G–H · 3758 Å² buried · 48 hydrogen bonds · protein-protein
B–C · 3744 Å² buried · 42 hydrogen bonds · protein-protein
F–J · 3724 Å² buried · 36 hydrogen bonds · protein-protein
C–D · 3720 Å² buried · 49 hydrogen bonds · protein-protein
A–E · 3705 Å² buried · 39 hydrogen bonds · protein-protein

Compared structures

2C6S · human adenovirus penton base 2 12 chimera · 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 P03276
Elsewhere: RCSB PDB 2C6S · PDBe 2C6S · UniProt P03276

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