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Structure of DNA helicase mutant with adpnp

Analyse Structure of DNA helicase mutant with adpnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QHG
Type: protein
Length: 622 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent helicase pcra
UniProt: P56255
Ligands: ATP, MG
Pockets: 7 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP-dependent helicase pcra	protein	622	53% helix, 13% strand	P56255

Ligands and binding sites

ATP · Adenosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

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

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1008	0.75	0.78	91	MG, ATP
2	263	0.56	0.77	29	empty
3	70	0.41	0.80	16	empty
4	58	0.35	0.78	15	empty
5	57	0.30	0.75	14	empty

Compared structures

1QHG · Structure of DNA helicase mutant with adpnp · the same entry in another collection · chain A against A, TM-score 1.00
P56255 · AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase pcra (P56255) · a predicted model of the same protein · chain A against A, TM-score 0.76

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 P56255
Elsewhere: RCSB PDB 1QHG · PDBe 1QHG · UniProt P56255

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