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Crystal structure of a putative O-methyltransferase from klebsiella pneumoniae

Analyse Crystal structure of a putative O-methyltransferase from klebsiella pneumoniae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3TFW
Type: protein
Length: 441 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative O-methyltransferase
UniProt: A6T8J6
Pockets: 5 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative O-methyltransferase	protein	221	46% helix, 19% strand	A6T8J6
B	Putative O-methyltransferase	protein	220	48% helix, 19% strand	A6T8J6

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	566	0.68	0.78	65	empty
2	633	0.67	0.76	54	empty
3	549	0.67	0.77	70	empty
4	84	0.48	0.82	20	empty
5	51	0.30	0.76	11	empty

Interfaces

1 interface between chains.

A–B · 598 Å² buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

3TFW · Crystal structure of a putative O-methyltransferase from Klebsiella pneumoniae · 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 A6T8J6
Elsewhere: RCSB PDB 3TFW · PDBe 3TFW · UniProt A6T8J6

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