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Crystal structure of human recq-like DNA helicase

Analyse Crystal structure of human recq-like DNA helicase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2V1X
Type: protein
Length: 1,054 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent DNA helicase Q1
EC: 3.6.1.-
UniProt: P46063
Ligands: ADP, MG, ZN, CL
Pockets: 11 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ATP-dependent DNA helicase Q1 (EC 3.6.1.-)	protein	527	43% helix, 17% strand	P46063

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B
CL · Chloride ion · ion · 9 copies · chains A, B
EDO · 1,2-ethanediol · additive · 2 copies · chains B

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

Pockets

11 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	775	0.74	0.79	70	ADP, MG, CL
2	825	0.72	0.77	70	ADP, MG, CL
3	413	0.64	0.78	45	CL
4	138	0.47	0.78	26	EDO
5	205	0.47	0.75	30	empty

Interfaces

1 interface between chains.

A–B · 432 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

2V1X · Crystal structure of human RECQ-like DNA helicase · the same entry in another collection · chain A against A, TM-score 1.00
P46063 · AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase Q1 (P46063) · a predicted model of the same protein · chain A against A, TM-score 0.91

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 P46063
Elsewhere: RCSB PDB 2V1X · PDBe 2V1X · UniProt P46063

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