MolNFT v1 · #71166 · protein

Crystal structure of the mutant V182A,V201A of orotidine 5'- monophosphate decarboxylase from methanobacterium thermoautotrophicum

3M5Y · Orotidine 5'-phosphate decarboxylase: “Crystal structure of the mutant V182A,V201A of orotidine 5'- monophosphate decarboxylase from…”. X-ray diffraction, 1 pocket (best druggability 0.78). MolNFT v1 #71166 on GenesisL1: 3D…

PDB: 3M5Y
Type: protein
Length: 424 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: O26232
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23)	protein	212	49% helix, 18% strand	O26232

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B
FMT · Formic acid · additive · 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	591	0.78	0.84	74	empty

Interfaces

1 interface between chains.

A–B · 1679 Å² buried · 23 hydrogen bonds · protein-protein

Compared structures

3M5Y · Crystal structure of the mutant V182A,V201A of orotidine 5'-monophosphate decarboxylase… · 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 O26232
Elsewhere: RCSB PDB 3M5Y · PDBe 3M5Y · UniProt O26232

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