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Early E2A DNA-binding protein

Analyse Early E2A DNA-binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ADV
Type: protein
Length: 573 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Adenovirus single-stranded DNA-binding protein
UniProt: P03265
Ligands: ZN
Pockets: 8 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Adenovirus single-stranded DNA-binding protein	protein	287	37% helix, 11% strand	P03265
B	Adenovirus single-stranded DNA-binding protein	protein	286	38% helix, 10% strand	P03265

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

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

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	495	0.62	0.75	38	empty
2	80	0.61	0.89	25	empty
3	167	0.52	0.78	20	empty
4	125	0.43	0.77	23	empty
5	95	0.40	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 1466 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

1ADV · Early E2A DNA-binding protein · the same entry in another collection · chain B against B, 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 P03265
Elsewhere: RCSB PDB 1ADV · PDBe 1ADV · UniProt P03265

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