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Crystal structure of the reduced form of mycobacterium tuberculosis guanylate kinase in complex with GDP

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

PDB: 1ZNZ
Type: protein
Length: 183 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Guanylate kinase
EC: 2.7.4.8
UniProt: P0A5I4
Ligands: GDP
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Guanylate kinase (EC 2.7.4.8)	protein	183	44% helix, 22% strand	P0A5I4

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	186	0.45	0.75	32	GDP

Compared structures

1ZNZ · Crystal Structure Of The Reduced Form Of Mycobacterium tuberculosis Guanylate Kinase In… · 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 P0A5I4
Elsewhere: RCSB PDB 1ZNZ · PDBe 1ZNZ · UniProt P0A5I4

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