MolNFT v1 · #19683 · protein + DNA

X-ray structure of the DNA-eco ri endonuclease complexes with an E144D mutation at 2.7 a

1QRI · 5'-D(*TP*CP*GP*CP*GP*AP*AP*TP*TP*CP*GP*CP*G)-3': “X-ray structure of the DNA-eco ri endonuclease complexes with an E144D mutation at 2.7 a”. X-ray diffraction, 3 pockets (best druggability 0.41). MolNFT v1 #19683 on GenesisL1: 3D…

PDB: 1QRI
Type: protein + DNA
Length: 274 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5'-D(*TP*CP*GP*CP*GP*AP*AP*TP*TP*CP*GP*CP*G)-3'; Eco ri endonculease
UniProt: P00642
Pockets: 3 · best druggability 0.41

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
M	5'-D(TPCPGPCPGPAPAPTPTPCPGPCP*G)-3'	dna	13	—	—
A	Eco ri endonculease	protein	261	33% helix, 20% strand	P00642

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.41	0.77	18	empty
2	58	0.31	0.76	17	empty
3	56	0.26	0.73	16	empty

Interfaces

1 interface between chains.

M–A · 814 Å² buried · 16 hydrogen bonds · protein-nucleic

Compared structures

1QRI · X-ray structure of the DNA-eco ri endonuclease complexes with an E144D mutation at 2.7 a · the same entry in another collection · chain M against M, TM-score 1.00
P00642 · AlphaFold monomer V2.0 prediction for type-2 restriction enzyme ecori (P00642) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P00642
Elsewhere: RCSB PDB 1QRI · PDBe 1QRI · UniProt P00642

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