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Crystal structure of E. COLI uvrd

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

PDB: 3LFU
Type: protein
Length: 633 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA helicase II
EC: 3.6.1.-
UniProt: P03018
Ligands: SO4
Pockets: 7 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA helicase II (EC 3.6.1.-)	protein	633	53% helix, 14% strand	P03018

Ligands and binding sites

SO4 · Sulfate ion · ion · 4 copies · 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	929	0.77	0.80	110	empty
2	286	0.58	0.78	37	SO4
3	90	0.41	0.78	19	SO4
4	98	0.37	0.75	18	empty
5	107	0.36	0.74	19	empty

Compared structures

3LFU · Crystal Structure of E. coli UvrD · the same entry in another collection · chain A against A, TM-score 1.00
P03018 · AlphaFold monomer V2.0 prediction for DNA helicase II (P03018) · a predicted model of the same protein · chain A against A, TM-score 0.70

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 P03018
Elsewhere: RCSB PDB 3LFU · PDBe 3LFU · UniProt P03018

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