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Structure and inhibition of orotidine 5'-phosphate decarboxylase from plasmodium falciparum

Analyse Structure and inhibition of orotidine 5'-phosphate decarboxylase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZCG
Type: protein
Length: 633 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Orotidine 5'-phosphate decarboxylase
EC: 4.1.1.23
UniProt: Q8T6J6
Pockets: 8 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23)	protein	318	53% helix, 15% strand	Q8T6J6
B	Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23)	protein	315	53% helix, 15% strand	Q8T6J6

Pockets

8 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	134	0.67	0.89	35	empty
2	202	0.67	0.85	41	empty
3	61	0.38	0.80	15	empty
4	91	0.37	0.76	15	empty
5	87	0.36	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 2437 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

2ZCG · Structure and inhibition of orotidine 5'-phosphate decarboxylase from plasmodium… · 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 Q8T6J6
Elsewhere: RCSB PDB 2ZCG · PDBe 2ZCG · UniProt Q8T6J6

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