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UTP cyclohydrolase

Analyse UTP cyclohydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7EEV
Type: protein
Length: 796 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTP cyclohydrolase II
UniProt: A0A3D9R4E8
Ligands: DUT, ZN
Pockets: 13 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTP cyclohydrolase II	protein	397	38% helix, 14% strand	A0A3D9R4E8
B	GTP cyclohydrolase II	protein	399	37% helix, 14% strand	A0A3D9R4E8

Ligands and binding sites

DUT · Deoxyuridine-5'-triphosphate · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B

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

Pockets

13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	186	0.83	0.97	33	DUT, ZN
2	198	0.82	0.96	38	empty
3	173	0.81	0.97	32	DUT
4	96	0.78	0.98	28	empty
5	105	0.77	0.97	29	empty

Interfaces

1 interface between chains.

A–B · 4862 Å² buried · 54 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 covalent (covalent ligand).

Compared structures

7EEV · Structure of UTP cyclohydrolase · 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 A0A3D9R4E8
Elsewhere: RCSB PDB 7EEV · PDBe 7EEV · UniProt A0A3D9R4E8

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