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Structure of a methyltransferase complex

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

PDB: 5Y4S
Type: protein
Length: 2,697 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chemotaxis protein methyltransferase 1
EC: 2.1.1.80
UniProt: O87131
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 3 distinct chains · 39% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, E, F, G, H, I, J	Chemotaxis protein methyltransferase 1 (EC 2.1.1.80)	protein	270	38% helix, 19% strand	O87131
B	Chemotaxis protein methyltransferase 1 (EC 2.1.1.80)	protein	269	39% helix, 18% strand	O87131
D	Chemotaxis protein methyltransferase 1 (EC 2.1.1.80)	protein	268	41% helix, 18% strand	O87131

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	807	0.86	0.89	157	empty
2	1035	0.83	0.84	133	empty
3	603	0.81	0.86	99	empty
4	499	0.80	0.87	86	empty
5	328	0.76	0.87	48	empty

Interfaces

19 interfaces between chains.

C–D · 1297 Å² buried · 16 hydrogen bonds · protein-protein
B–H · 1244 Å² buried · 10 hydrogen bonds · protein-protein
I–J · 1234 Å² buried · 1 hydrogen bond · protein-protein
G–H · 954 Å² buried · 6 hydrogen bonds · protein-protein
F–I · 933 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5Y4S · Structure of a methyltransferase complex · the same entry in another collection · chain J against J, TM-score 1.00
O87131 · AlphaFold monomer V2.0 prediction for chemotaxis protein methyltransferase 1 (O87131) · a predicted model of the same protein · chain A against A, TM-score 0.75

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 O87131
Elsewhere: RCSB PDB 5Y4S · PDBe 5Y4S · UniProt O87131

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