MolNFT v1 · #142378 · protein

Apo structure of the kdo hydroxylase kdoo, a non-heme FE(II) alphaketoglutarate dependent dioxygenase

6A2E · Kdo hydroxylase, kdoo: “Apo structure of the kdo hydroxylase kdoo, a non-heme FE(II) alphaketoglutarate dependent dioxygenase”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.71). MolNFT v1 #142378 on GenesisL1…

PDB: 6A2E
Type: protein
Length: 296 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kdo hydroxylase, kdoo
UniProt: B3DUR4
Ligands: SO4
Pockets: 3 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kdo hydroxylase, kdoo	protein	296	36% helix, 20% strand	B3DUR4

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A
ACT · Acetate ion · additive · 3 copies · chains A
PG4 · Tetraethylene glycol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	554	0.71	0.80	54	ACT
2	69	0.33	0.76	12	empty
3	51	0.30	0.76	17	empty

Compared structures

6A2E · Apo structure of the Kdo hydroxylase KdoO, a non-heme Fe(II) alphaketoglutarate dependent… · 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 B3DUR4
Elsewhere: RCSB PDB 6A2E · PDBe 6A2E · UniProt B3DUR4

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