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Crystal structure of arna dehydrogenase (decarboxylase) domain, R619M mutant

Analyse Crystal structure of arna dehydrogenase (decarboxylase) domain, R619M mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Z75
Type: protein
Length: 334 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein arna
UniProt: P77398
Ligands: SO4
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein arna	protein	334	44% helix, 19% strand	P77398

Ligands and binding sites

SO4 · Sulfate ion · ion · 2 copies · chains A
GOL · Glycerol · 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	531	0.74	0.82	44	SO4
2	111	0.39	0.75	24	empty
3	66	0.35	0.77	15	empty

Compared structures

1Z75 · Crystal Structure of ArnA dehydrogenase (decarboxylase) domain, R619M mutant · the same entry in another collection · chain A against A, TM-score 1.00
P77398 · AlphaFold monomer V2.0 prediction for bifunctional polymyxin resistance protein arna… · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P77398
Elsewhere: RCSB PDB 1Z75 · PDBe 1Z75 · UniProt P77398

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