MolNFT v1 · #58023 · protein

Complex structure of bacterial protein (apo form II)

3AQN · POLY(A) polymerase: “Complex structure of bacterial protein (apo form II)”. X-ray diffraction, 2 ligands (ATP, MG), 5 pockets (best druggability 0.73). MolNFT v1 #58023 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3AQN
Type: protein
Length: 776 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: POLY(A) polymerase
EC: 2.7.7.19
UniProt: C9QS13
Ligands: ATP, MG
Pockets: 5 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	POLY(A) polymerase (EC 2.7.7.19)	protein	388	56% helix, 9% strand	C9QS13

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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	622	0.73	0.80	48	empty
2	468	0.62	0.76	37	ATP, MG
3	496	0.62	0.75	46	ATP, MG
4	286	0.52	0.74	40	empty
5	58	0.33	0.77	16	empty

Interfaces

1 interface between chains.

A–B · 994 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

3AQN · Complex structure of bacterial protein (apo form II) · 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 C9QS13
Elsewhere: RCSB PDB 3AQN · PDBe 3AQN · UniProt C9QS13

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