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Crystal structure of spectinomycin phosphotransferase, APH(9)-ia, protein kinase inhibitor cki-7 complex

Analyse Crystal structure of spectinomycin phosphotransferase, APH(9)-ia, protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3Q2M
Type: protein
Length: 329 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Spectinomycin phosphotransferase
UniProt: E1XXQ2
Ligands: CKI, NI
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Spectinomycin phosphotransferase	protein	329	44% helix, 15% strand	E1XXQ2

Ligands and binding sites

CKI · N-(2-aminoethyl)-5-chloroisoquinoline-8-sulfonamide · ligand · chains A
NI · Nickel (II) ion · metal · chains A

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

Pockets

3 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	771	0.74	0.79	73	CKI
2	64	0.37	0.78	15	empty
3	64	0.30	0.74	15	empty

Compared structures

3Q2M · Crystal Structure of Spectinomycin Phosphotransferase, APH(9)-Ia, Protein Kinase… · 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 E1XXQ2
Elsewhere: RCSB PDB 3Q2M · PDBe 3Q2M · UniProt E1XXQ2

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