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Structure of the recq catalytic core

Analyse Structure of the recq catalytic core in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OYW
Type: protein
Length: 516 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ATP-dependent DNA helicase
EC: 3.6.1.-
UniProt: P15043
Ligands: ZN, MN
Pockets: 5 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ATP-dependent DNA helicase (EC 3.6.1.-)	protein	516	46% helix, 15% strand	P15043

Ligands and binding sites

ZN · Zinc ion · metal · chains A
MN · Manganese (II) 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	774	0.73	0.79	84	empty
2	266	0.64	0.81	44	empty
3	106	0.43	0.77	23	empty
4	88	0.37	0.76	18	empty
5	50	0.37	0.80	12	empty

Modifications

Observed in the structure: 15 modified (engineered).

Compared structures

1OYW · Structure of the RecQ Catalytic Core · the same entry in another collection · chain A against A, TM-score 1.00
P15043 · AlphaFold monomer V2.0 prediction for ATP-dependent DNA helicase recq (P15043) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P15043
Elsewhere: RCSB PDB 1OYW · PDBe 1OYW · UniProt P15043

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