MolNFT v1 · #105133 · protein

Apo-crystal structure of podospora anserina methyltransferase PAMTH1

4QVK · PAMTH1 methyltransferase: “Apo-crystal structure of podospora anserina methyltransferase PAMTH1”. X-ray diffraction, 5 pockets (best druggability 0.79). MolNFT v1 #105133 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4QVK
Type: protein
Length: 470 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: PAMTH1 methyltransferase
UniProt: Q9HGR1
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	PAMTH1 methyltransferase	protein	235	46% helix, 19% strand	Q9HGR1

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

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

Pockets

5 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	124	0.79	0.97	25	empty
2	357	0.71	0.83	53	empty
3	365	0.68	0.81	54	empty
4	63	0.43	0.82	15	empty
5	127	0.41	0.76	17	empty

Interfaces

1 interface between chains.

A–B · 3204 Å² buried · 34 hydrogen bonds · protein-protein

Compared structures

4QVK · Apo-crystal structure of Podospora anserina methyltransferase PaMTH1 · the same entry in another collection · chain A against A, TM-score 1.00

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 Q9HGR1
Elsewhere: RCSB PDB 4QVK · PDBe 4QVK · UniProt Q9HGR1

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