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Inhibitory human GTP cyclohydrolase I - gfrp complex

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

PDB
6Z85
Type
protein
Length
2,360 residues
Chains
20
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GTP cyclohydrolase 1; GTP cyclohydrolase 1 feedback regulatory protein
EC
3.5.4.16
UniProt
P30793, P30047
Ligands
HBI, ZN
Pockets
20 · best druggability 0.88

Structure

electron microscopy · 2 distinct chains · 33% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, D, B, E, G, H, I, J, FGTP cyclohydrolase 1 (EC 3.5.4.16)protein15541% helix, 28% strandP30793
K, L, M, N, O, P, Q, R, S, TGTP cyclohydrolase 1 feedback regulatory proteinprotein8120% helix, 36% strandP30047

Ligands and binding sites

  • HBI · 7,8-dihydrobiopterin · ligand · 10 copies · chains A, E, C, B, D, G, F, H, I, J
  • ZN · Zinc ion · metal · 10 copies · chains A, C, D, B, E, G, H, I, J, F

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19700.880.90106HBI
27010.870.9191HBI
3920.780.9822empty
4990.780.9722empty
5920.770.9722empty

Interfaces

55 interfaces between chains.

  • D–H · 1506 Ų buried · 7 hydrogen bonds · protein-protein
  • C–I · 1502 Ų buried · 8 hydrogen bonds · protein-protein
  • E–G · 1494 Ų buried · 6 hydrogen bonds · protein-protein
  • A–F · 1492 Ų buried · 6 hydrogen bonds · protein-protein
  • B–J · 1487 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 6Z85 · inhibitory human GTP cyclohydrolase I - GFRP complex · the same entry in another collection · chain T against T, TM-score 1.00

Analyse

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