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Human orotidyl-5'-monophosphate decarboxylase in complex with 6-cyano- ump

Analyse Human orotidyl-5'-monophosphate decarboxylase in complex with 6-cyano- ump in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3EX2
Type: protein
Length: 514 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: P11172
Ligands: 6CN
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Orotidine-5'-phosphate decarboxylase (EC 4.1.1.23)	protein	257	44% helix, 18% strand	P11172

Ligands and binding sites

6CN · 6-cyanouridine 5'-phosphate · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · chains A

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

Pockets

2 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	133	0.74	0.93	31	6CN
2	125	0.72	0.93	31	6CN

Interfaces

1 interface between chains.

A–B · 1968 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

3EX2 · human orotidyl-5'-monophosphate decarboxylase in complex with 6-cyano-UMP · 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 P11172
Elsewhere: RCSB PDB 3EX2 · PDBe 3EX2 · UniProt P11172

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