MolNFT v1 · #23834 · protein

Crystal structure of a lysine biosynthesis enzyme, lysx, from thermus thermophilus HB8

1UC9: “Crystal structure of a lysine biosynthesis enzyme, lysx, from thermus thermophilus HB8”. X-ray diffraction, 1 ligand (ADP), 4 pockets (best druggability 0.63). MolNFT v1 #23834 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 1UC9
Type: protein
Length: 509 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysine biosynthesis enzyme
UniProt: Q84BR0
Ligands: ADP
Pockets: 4 · best druggability 0.63

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysine biosynthesis enzyme	protein	256	38% helix, 27% strand	Q84BR0
B	Lysine biosynthesis enzyme	protein	253	38% helix, 26% strand	Q84BR0

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

4 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	79	0.63	0.90	18	empty
2	252	0.55	0.78	33	empty
3	137	0.44	0.77	23	empty
4	133	0.41	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 1895 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

1UC9 · Crystal structure of a lysine biosynthesis enzyme, Lysx, from thermus thermophilus HB8 · 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 Q84BR0
Elsewhere: RCSB PDB 1UC9 · PDBe 1UC9 · UniProt Q84BR0

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