MolNFT v1 · #107895 · protein

Crystal structure of listeria monocytogenes GTP cyclohydrolase I

4UQF · GTP cyclohydrolase 1: “Crystal structure of listeria monocytogenes GTP cyclohydrolase I”. X-ray diffraction, 20 pockets (best druggability 0.82). MolNFT v1 #107895 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4UQF
Type: protein
Length: 1,860 residues
Chains: 10
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTP cyclohydrolase 1
EC: 3.5.4.16
UniProt: A0A1D2IZD1
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	GTP cyclohydrolase 1 (EC 3.5.4.16)	protein	186	45% helix, 25% strand	A0A1D2IZD1

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1132	0.82	0.83	174	empty
2	730	0.81	0.85	42	empty
3	252	0.79	0.91	33	empty
4	795	0.79	0.82	41	empty
5	743	0.78	0.82	114	empty

Interfaces

25 interfaces between chains.

D–G · 2034 Å² buried · 15 hydrogen bonds · protein-protein
E–I · 2012 Å² buried · 13 hydrogen bonds · protein-protein
H–J · 2002 Å² buried · 13 hydrogen bonds · protein-protein
A–F · 1988 Å² buried · 16 hydrogen bonds · protein-protein
B–C · 1986 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

4UQF · Crystal structure of listeria monocytogenes GTP cyclohydrolase I · 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 A0A1D2IZD1
Elsewhere: RCSB PDB 4UQF · PDBe 4UQF · UniProt A0A1D2IZD1

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