MolNFT v1 · #135442 · protein

Crystal structure of curk dehydratase D1169N inactive mutant

5TZ7: “Crystal structure of curk dehydratase D1169N inactive mutant”. X-ray diffraction, 5 pockets (best druggability 0.75). MolNFT v1 #135442 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5TZ7
Type: protein
Length: 556 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Curk
UniProt: F4Y425
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Curk	protein	277	21% helix, 43% strand	F4Y425
B	Curk	protein	279	24% helix, 42% strand	F4Y425

Ligands and binding sites

FLC · Citrate anion · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	187	0.75	0.91	38	empty
2	258	0.71	0.86	50	empty
3	96	0.51	0.83	22	empty
4	67	0.50	0.85	19	empty
5	77	0.31	0.74	18	empty

Interfaces

1 interface between chains.

A–B · 727 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

5TZ7 · Crystal Structure of CurK Dehydratase D1169N Inactive Mutant · 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 F4Y425
Elsewhere: RCSB PDB 5TZ7 · PDBe 5TZ7 · UniProt F4Y425

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