MolNFT v1 · #58021 · protein

Structure of bacterial protein (apo form II)

3AQL · POLY(A) polymerase: “Structure of bacterial protein (apo form II)”. X-ray diffraction, 1 ligand (MG), 4 pockets (best druggability 0.74). MolNFT v1 #58021 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3AQL
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: MG
Pockets: 4 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	POLY(A) polymerase (EC 2.7.7.19)	protein	388	55% helix, 8% strand	C9QS13

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

4 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	636	0.74	0.81	50	empty
2	490	0.63	0.76	38	MG, GOL
3	455	0.61	0.76	45	GOL
4	289	0.55	0.76	42	empty

Interfaces

1 interface between chains.

A–B · 1023 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

3AQL · 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 3AQL · PDBe 3AQL · UniProt C9QS13

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