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Structure of the cyanuric acid hydrolase trzd reveals product exit channel

Analyse Structure of the cyanuric acid hydrolase trzd reveals product exit channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T13
Type: protein
Length: 376 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyanuric acid amidohydrolase
EC: 3.5.2.15
UniProt: P0A3V4
Ligands: MG, CO2
Pockets: 2 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyanuric acid amidohydrolase (EC 3.5.2.15)	protein	376	33% helix, 28% strand	P0A3V4

Ligands and binding sites

MG · Magnesium ion · metal · chains A
CO2 · Carbon dioxide · ion · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	120	0.42	0.76	21	empty
2	57	0.29	0.75	12	empty

Compared structures

5T13 · Structure of the Cyanuric Acid Hydrolase TrzD Reveals Product Exit Channel · the same entry in another collection · chain A against A, TM-score 1.00
P0A3V4 · AlphaFold monomer V2.0 prediction for cyanuric acid amidohydrolase (P0A3V4) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P0A3V4
Elsewhere: RCSB PDB 5T13 · PDBe 5T13 · UniProt P0A3V4

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