MolNFT v1 · #63028 · protein

Human orotidyl-5'-monophosphate decarboxylase in complex with bmp

3EX4 · Orotidine-5'-phosphate decarboxylase: “Human orotidyl-5'-monophosphate decarboxylase in complex with bmp”. X-ray diffraction, 1 ligand (BMP), 1 pocket (best druggability 0.52). MolNFT v1 #63028 on GenesisL1: 3D structure, binding…

PDB: 3EX4
Type: protein
Length: 257 residues
Chains: 1
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: BMP
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Orotidine-5'-phosphate decarboxylase (EC 4.1.1.23)	protein	257	45% helix, 17% strand	P11172

Ligands and binding sites

BMP · 6-hydroxyuridine-5'-phosphate · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	166	0.52	0.79	27	BMP

Compared structures

3EX4 · human orotidyl-5'-monophosphate decarboxylase in complex with BMP · 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 3EX4 · PDBe 3EX4 · UniProt P11172

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