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Crystal structure of aminoglycoside-3'-phosphotransferase of type VIII

Analyse Crystal structure of aminoglycoside-3'-phosphotransferase of type VIII in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4H05
Type: protein
Length: 541 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminoglycoside-O-phosphotransferase VIII
EC: 2.7.1.95
UniProt: Q9F9M5
Pockets: 6 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Aminoglycoside-O-phosphotransferase VIII (EC 2.7.1.95)	protein	270	43% helix, 20% strand	Q9F9M5
B	Aminoglycoside-O-phosphotransferase VIII (EC 2.7.1.95)	protein	271	42% helix, 18% strand	Q9F9M5

Pockets

6 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	191	0.60	0.82	33	empty
2	409	0.60	0.76	48	empty
3	155	0.54	0.80	23	empty
4	68	0.46	0.83	15	empty
5	161	0.41	0.73	28	empty

Interfaces

1 interface between chains.

A–B · 873 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4H05 · Crystal structure of aminoglycoside-3'-phosphotransferase of type VIII · 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 Q9F9M5
Elsewhere: RCSB PDB 4H05 · PDBe 4H05 · UniProt Q9F9M5

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