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Structure of unliganded and reductively methylated FHUD2 from staphylococcus aureus

Analyse Structure of unliganded and reductively methylated FHUD2 from staphylococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4FKM
Type: protein
Length: 513 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Similar to ferric hydroxamate receptor 1
UniProt: Q99RY8
Pockets: 2 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 47% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Similar to ferric hydroxamate receptor 1	protein	256	46% helix, 18% strand	Q99RY8
B	Similar to ferric hydroxamate receptor 1	protein	257	47% helix, 16% strand	Q99RY8

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.60	0.87	18	empty
2	88	0.38	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 1049 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 96 modified (methylation, engineered).

Compared structures

4FKM · Structure of unliganded and reductively methylated FhuD2 from staphylococcus aureus · 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 Q99RY8
Elsewhere: RCSB PDB 4FKM · PDBe 4FKM · UniProt Q99RY8

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