MolNFT v1 · #10462 · protein

Crystal structure of rat GTPCHI/GFRP stimulatory complex

1IS7 · GTP cyclohydrolase I: “Crystal structure of rat GTPCHI/GFRP stimulatory complex”. X-ray diffraction, 2 ligands (PHE, K), 20 pockets (best druggability 0.83). MolNFT v1 #10462 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1IS7
Type: protein
Length: 2,780 residues
Chains: 20
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTP cyclohydrolase I; GTP cyclohydrolase I feedback regulatory protein
EC: 3.5.4.16
UniProt: P22288, P70552
Ligands: PHE, K
Pockets: 20 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	GTP cyclohydrolase I (EC 3.5.4.16)	protein	194	45% helix, 28% strand	P22288
K, L, M, N, O, P, Q, R, S, T	GTP cyclohydrolase I feedback regulatory protein	protein	84	20% helix, 40% strand	P70552

Ligands and binding sites

PHE · Phenylalanine · ligand · 10 copies · chains A, K, L, B, M, C, N, D, O, E, F, P, Q, G, R, H, S, I, T, J
K · Potassium ion · metal · 10 copies · chains K, L, M, N, O, P, Q, R, S, T

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	349	0.83	0.92	66	PHE
2	90	0.79	0.99	22	empty
3	94	0.79	0.98	24	empty
4	92	0.78	0.98	21	empty
5	91	0.78	0.98	22	empty

Interfaces

55 interfaces between chains.

E–F · 2023 Å² buried · 12 hydrogen bonds · protein-protein
C–H · 2008 Å² buried · 12 hydrogen bonds · protein-protein
D–G · 2007 Å² buried · 12 hydrogen bonds · protein-protein
B–I · 2003 Å² buried · 12 hydrogen bonds · protein-protein
A–J · 1994 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

1IS7 · Crystal structure of rat GTPCHI/GFRP stimulatory complex · the same entry in another collection · chain J against J, 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 P22288
Every structure of UniProt P70552
Elsewhere: RCSB PDB 1IS7 · PDBe 1IS7 · UniProt P22288 · UniProt P70552

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