MolNFT v1 · #120271 · protein

The crystal structure of mouse DNMT1 (731-1602) mutant - R1279D

5GUV · DNA (cytosine-5)-methyltransferase 1: “The crystal structure of mouse DNMT1 (731-1602) mutant - R1279D”. X-ray diffraction, 1 ligand (ZN), 8 pockets (best druggability 0.70). MolNFT v1 #120271 on GenesisL1: 3D structure, binding…

PDB: 5GUV
Type: protein
Length: 818 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA (cytosine-5)-methyltransferase 1
EC: 2.1.1.37
UniProt: P13864
Ligands: ZN
Pockets: 8 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA (cytosine-5)-methyltransferase 1 (EC 2.1.1.37)	protein	818	23% helix, 27% strand	P13864

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Pockets

8 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	620	0.70	0.78	53	empty
2	306	0.58	0.77	44	empty
3	191	0.56	0.80	28	empty
4	147	0.47	0.77	22	empty
5	122	0.44	0.77	21	empty

Compared structures

5GUV · The crystal structure of mouse DNMT1 (731-1602) mutant - R1279D · the same entry in another collection · chain A against A, TM-score 1.00
P13864 · AlphaFold monomer V2.0 prediction for DNA (cytosine-5)-methyltransferase 1 (P13864) · 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 P13864
Elsewhere: RCSB PDB 5GUV · PDBe 5GUV · UniProt P13864

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