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Structure of putative orotidine-monophosphate-decarboxylase from plasmodium yoelii (PY01515)

Analyse Structure of putative orotidine-monophosphate-decarboxylase from plasmodium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2AQW
Type: protein
Length: 321 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative orotidine-monophosphate-decarboxylase
UniProt: Q7RPE4
Ligands: IOD, SO4
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative orotidine-monophosphate-decarboxylase	protein	321	55% helix, 15% strand	Q7RPE4

Ligands and binding sites

IOD · Iodide ion · ion · 6 copies · chains A
SO4 · Sulfate ion · ion · 3 copies · 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	121	0.52	0.81	27	IOD, SO4
2	127	0.42	0.75	25	empty
3	80	0.32	0.73	14	empty

Modifications

Observed in the structure: 11 modified (engineered).

Compared structures

2AQW · Structure of putative orotidine-monophosphate-decarboxylase from Plasmodium yoelii… · 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 Q7RPE4
Elsewhere: RCSB PDB 2AQW · PDBe 2AQW · UniProt Q7RPE4

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