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Crystal structure of orotidine 5-phosphate decarboxylase from anaerococcus prevotii dsm 20548

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

PDB: 3R89
Type: protein
Length: 578 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: C7RH50
Pockets: 4 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23)	protein	289	51% helix, 17% strand	C7RH50

Pockets

4 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	349	0.64	0.79	35	empty
2	324	0.62	0.79	39	empty
3	52	0.27	0.75	15	empty
4	62	0.27	0.73	16	empty

Interfaces

1 interface between chains.

A–B · 2368 Å² buried · 39 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

3R89 · Crystal structure of orotidine 5-phosphate decarboxylase from Anaerococcus prevotii DSM… · the same entry in another collection · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt C7RH50
Elsewhere: RCSB PDB 3R89 · PDBe 3R89 · UniProt C7RH50

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