MolNFT v1 · #145639 · protein

Structure of the GDP and kanamycin complex of APH(2")-iiia

6CTZ · Gentamicin resistance protein: “Structure of the GDP and kanamycin complex of APH(2")-iiia”. X-ray diffraction, 4 ligands (GDP, KAN, MG), 2 pockets (best druggability 0.72). MolNFT v1 #145639 on GenesisL1: 3D structure, binding…

PDB: 6CTZ
Type: protein
Length: 297 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Gentamicin resistance protein
UniProt: P96762
Ligands: GDP, KAN, MG, CL
Pockets: 2 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Gentamicin resistance protein	protein	297	56% helix, 17% strand	P96762

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · chains A
KAN · Kanamycin A · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A
CL · Chloride ion · ion · 2 copies · chains A

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

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	655	0.72	0.79	56	GDP, MG, KAN, CL
2	82	0.33	0.74	14	empty

Compared structures

6CTZ · Structure of the GDP and kanamycin complex of APH(2)-IIia" · 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 P96762
Elsewhere: RCSB PDB 6CTZ · PDBe 6CTZ · UniProt P96762

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