MolNFT v1 · #171521 · protein
Human GTP cyclohydrolase I in complex with 7-deaza-GTP
6Z86 · GTP cyclohydrolase 1: “Human GTP cyclohydrolase I in complex with 7-deaza-GTP”. X-ray diffraction, 2 ligands (QBQ, ZN), 20 pockets (best druggability 0.79). MolNFT v1 #171521 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6Z86
- Type
- protein
- Length
- 3,813 residues
- Chains
- 20
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- GTP cyclohydrolase 1
- EC
- 3.5.4.16
- UniProt
- P30793
- Ligands
- QBQ, ZN
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 10 distinct chains · 46% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, I | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 192 | 46% helix, 28% strand | P30793 |
| B, E, F, J, Q | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 190 | 46% helix, 28% strand | P30793 |
| C, L, M | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 191 | 46% helix, 28% strand | P30793 |
| D | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 191 | 46% helix, 28% strand | P30793 |
| G, N | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 193 | 46% helix, 28% strand | P30793 |
| H, K | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 192 | 46% helix, 28% strand | P30793 |
| O, R | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 191 | 46% helix, 28% strand | P30793 |
| P | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 189 | 46% helix, 29% strand | P30793 |
| S | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 188 | 47% helix, 24% strand | P30793 |
| T | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 186 | 45% helix, 29% strand | P30793 |
Ligands and binding sites
- QBQ · 7-deaza-GTP · ligand · 20 copies · chains A, O, Q, B, C, D, P, T, E, J, L, F, H, M, G, K, N, I, R, S
- ZN · Zinc ion · metal · 20 copies · chains A, B, C, D, E, F, G, H, I, J, 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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1022 | 0.79 | 0.80 | 95 | empty |
| 2 | 1011 | 0.77 | 0.79 | 107 | empty |
| 3 | 73 | 0.77 | 0.99 | 23 | empty |
| 4 | 944 | 0.76 | 0.79 | 89 | empty |
| 5 | 60 | 0.75 | 0.99 | 22 | empty |
Interfaces
51 interfaces between chains.
- A–B · 1994 Ų buried · 15 hydrogen bonds · protein-protein
- E–I · 1987 Ų buried · 15 hydrogen bonds · protein-protein
- K–N · 1984 Ų buried · 16 hydrogen bonds · protein-protein
- F–G · 1981 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 1973 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 6Z86 · human GTP cyclohydrolase I in complex with 7-deaza-GTP · the same entry in another collection · chain K against K, 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 P30793
- Elsewhere: RCSB PDB 6Z86 · PDBe 6Z86 · UniProt P30793
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