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Crystal structure of dihydroorotase from thermus thermophilus

Analyse Crystal structure of dihydroorotase from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Z00
Type: protein
Length: 426 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydroorotase
EC: 3.5.2.3
UniProt: Q5SK67
Ligands: ZN
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydroorotase (EC 3.5.2.3)	protein	426	36% helix, 23% strand	Q5SK67

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	237	0.53	0.77	34	ZN
2	67	0.45	0.82	18	empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2Z00 · Crystal structure of dihydroorotase from Thermus thermophilus · the same entry in another collection · chain A against A, TM-score 1.00
Q5SK67 · AlphaFold monomer V2.0 prediction for dihydroorotase (Q5SK67) · a predicted model of the same protein · 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 Q5SK67
Elsewhere: RCSB PDB 2Z00 · PDBe 2Z00 · UniProt Q5SK67

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