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Crystal structure of mycobacterium tuberculosis thymidylate kinase complexed with bisubstrate inhibitor (TP5A)

Analyse Crystal structure of mycobacterium tuberculosis thymidylate kinase complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MRN
Type: protein
Length: 208 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thymidylate kinase
EC: 2.7.4.9
UniProt: O05891
Ligands: T5A, MG, SO4
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Thymidylate kinase (EC 2.7.4.9)	protein	208	55% helix, 11% strand	O05891

Ligands and binding sites

T5A · P1-(5'-adenosyl)p5-(5'-thymidyl)pentaphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A
SO4 · Sulfate ion · ion · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	331	0.69	0.83	38	SO4, MG, T5A

Compared structures

1MRN · Crystal structure of mycobacterium tuberculosis thymidylate kinase complexed with… · 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 O05891
Elsewhere: RCSB PDB 1MRN · PDBe 1MRN · UniProt O05891

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