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Structure of S. aureus methicillin resistance factor MECR2

Analyse Structure of S. aureus methicillin resistance factor MECR2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4IJA
Type: protein
Length: 724 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylr protein
UniProt: Q99XE2
Ligands: K, PO4
Pockets: 14 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Xylr protein	protein	363	42% helix, 23% strand	Q99XE2
B	Xylr protein	protein	361	42% helix, 24% strand	Q99XE2

Ligands and binding sites

K · Potassium ion · metal · 4 copies · chains A, B
PO4 · Phosphate ion · ion · chains A
GOL · Glycerol · additive · 6 copies · chains A, B

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

Pockets

14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	298	0.77	0.88	43	GOL
2	93	0.63	0.90	21	empty
3	180	0.54	0.79	26	K
4	208	0.53	0.78	23	empty
5	186	0.52	0.78	27	empty

Interfaces

1 interface between chains.

A–B · 1564 Å² buried · 35 hydrogen bonds · protein-protein

Compared structures

4IJA · Structure of S. aureus methicillin resistance factor MecR2 · 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 Q99XE2
Elsewhere: RCSB PDB 4IJA · PDBe 4IJA · UniProt Q99XE2

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