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Crystal structure of the aquifex aeolicus primase (zinc binding and RNA polymerase domains)

Analyse Crystal structure of the aquifex aeolicus primase (zinc binding and RNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AU3
Type: protein
Length: 403 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA primase
EC: 2.7.7.-
UniProt: O67465
Ligands: ZN
Pockets: 5 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA primase (EC 2.7.7.-)	protein	403	49% helix, 15% strand	O67465

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	800	0.74	0.79	66	empty
2	77	0.42	0.80	17	empty
3	55	0.42	0.82	15	empty
4	103	0.37	0.75	20	empty
5	54	0.34	0.78	13	empty

Compared structures

2AU3 · Crystal Structure of the Aquifex aeolicus primase (Zinc Binding and RNA Polymerase… · the same entry in another collection · chain A against A, TM-score 1.00
O67465 · AlphaFold monomer V2.0 prediction for DNA primase (O67465) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 O67465
Elsewhere: RCSB PDB 2AU3 · PDBe 2AU3 · UniProt O67465

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