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Crystal structure of the antibiotic-resistance methyltransferase kmr

Analyse Crystal structure of the antibiotic-resistance methyltransferase kmr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RWZ
Type: protein
Length: 390 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative rRNA methyltransferase
EC: 2.1.1.179
UniProt: B2L3G9
Pockets: 5 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative rRNA methyltransferase (EC 2.1.1.179)	protein	195	36% helix, 30% strand	B2L3G9
B	Putative rRNA methyltransferase (EC 2.1.1.179)	protein	195	33% helix, 30% strand	B2L3G9

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	998	0.79	0.81	95	empty
2	155	0.53	0.80	25	empty
3	61	0.42	0.81	11	empty
4	53	0.37	0.79	12	empty
5	53	0.35	0.79	19	empty

Interfaces

1 interface between chains.

A–B · 956 Å² buried · 14 hydrogen bonds · protein-protein

Compared structures

4RWZ · Crystal structure of the antibiotic-resistance methyltransferase Kmr · 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 B2L3G9
Elsewhere: RCSB PDB 4RWZ · PDBe 4RWZ · UniProt B2L3G9

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