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Crystal structure of human GTP cyclohydrolase I

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

PDB: 1FB1
Type: protein
Length: 980 residues
Chains: 5
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTP cyclohydrolase I
EC: 3.5.4.16
UniProt: P30793
Ligands: ZN
Pockets: 14 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	GTP cyclohydrolase I (EC 3.5.4.16)	protein	196	42% helix, 20% strand	P30793

Ligands and binding sites

ZN · Zinc ion · metal · 5 copies · chains A, B, C, D, E
IPA · Isopropyl alcohol · additive · 5 copies · chains A, B, C, D, E

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

Pockets

14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	653	0.77	0.82	58	empty
2	134	0.64	0.87	26	ZN, IPA
3	112	0.64	0.88	22	IPA
4	181	0.64	0.84	30	IPA
5	131	0.63	0.86	24	IPA

Interfaces

5 interfaces between chains.

C–D · 1277 Å² buried · 19 hydrogen bonds · protein-protein
A–E · 1266 Å² buried · 15 hydrogen bonds · protein-protein
B–C · 1252 Å² buried · 12 hydrogen bonds · protein-protein
A–B · 1239 Å² buried · 13 hydrogen bonds · protein-protein
D–E · 1234 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

1FB1 · Crystal structure of human GTP cyclohydrolase I · the same entry in another collection · chain E against E, TM-score 1.00
P30793 · AlphaFold monomer V2.0 prediction for GTP cyclohydrolase 1 (P30793) · 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 P30793
Elsewhere: RCSB PDB 1FB1 · PDBe 1FB1 · UniProt P30793

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