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Ump kinase from pyrococcus furiosus without ligands

Analyse Ump kinase from pyrococcus furiosus without ligands in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BRX
Type: protein
Length: 427 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uridylate kinase
EC: 2.7.4.-
UniProt: Q8U122
Pockets: 3 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uridylate kinase (EC 2.7.4.-)	protein	218	49% helix, 15% strand	Q8U122
B	Uridylate kinase (EC 2.7.4.-)	protein	209	51% helix, 16% strand	Q8U122

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	309	0.57	0.77	45	empty
2	260	0.55	0.77	35	empty
3	169	0.47	0.75	25	empty

Interfaces

1 interface between chains.

A–B · 1364 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2BRX · Ump kinase from pyrococcus furiosus without ligands · the same entry in another collection · chain A against A, TM-score 1.00
Q8U122 · AlphaFold monomer V2.0 prediction for uridylate kinase (Q8U122) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 Q8U122
Elsewhere: RCSB PDB 2BRX · PDBe 2BRX · UniProt Q8U122

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