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Solution NMR structure of the act domain from GTP pyrophosphokinase of chlorobium tepidum. northeast structural genomics consortium target CTR148A

Analyse Solution NMR structure of the act domain from GTP pyrophosphokinase of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2KO1
Type: protein
Length: 176 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTP pyrophosphokinase
EC: 2.7.6.5
UniProt: Q8KC80
Pockets: 1 · best druggability 0.46

Structure

solution nmr · 1 distinct chain · 23% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	GTP pyrophosphokinase (EC 2.7.6.5)	protein	88	23% helix, 40% strand	Q8KC80

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	158	0.46	0.76	26	empty

Interfaces

1 interface between chains.

A–B · 844 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

2KO1 · Solution NMR structure of the ACT domain from GTP pyrophosphokinase of Chlorobium… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8KC80
Elsewhere: RCSB PDB 2KO1 · PDBe 2KO1 · UniProt Q8KC80

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