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Crystal structure of the human RECQL4 helicase.

Analyse Crystal structure of the human RECQL4 helicase. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LST
Type: protein
Length: 617 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent DNA helicase Q4
EC: 3.6.4.12
UniProt: O94761
Ligands: ZN
Pockets: 11 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP-dependent DNA helicase Q4 (EC 3.6.4.12)	protein	617	41% helix, 17% strand	O94761

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

11 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	1143	0.77	0.79	105	empty
2	143	0.50	0.79	30	empty
3	260	0.49	0.74	48	empty
4	107	0.49	0.81	17	empty
5	173	0.44	0.74	28	empty

Compared structures

5LST · Crystal structure of the human RecQL4 helicase. · the same entry in another collection · chain A against A, TM-score 1.00
O94761 · AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase Q4 (O94761) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 O94761
Elsewhere: RCSB PDB 5LST · PDBe 5LST · UniProt O94761

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