MolNFT v1 · #173004 · protein
Human gch-gfrp stimulatory complex 7-deaza-GTP bound
7ALB · GTP cyclohydrolase 1: “Human gch-gfrp stimulatory complex 7-deaza-GTP bound”. X-ray diffraction, 3 ligands (QBQ, PHE, ZN), 20 pockets (best druggability 0.89). MolNFT v1 #173004 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 7ALB
- Type
- protein
- Length
- 5,478 residues
- Chains
- 40
- Method
- x-ray diffraction
- 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
- QBQ, PHE, ZN
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 10 distinct chains · 43% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E, K, O, P, Q, T | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 192 | 47% helix, 26% strand | P30793 |
| B, L | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 187 | 47% helix, 27% strand | P30793 |
| C, I, M, S | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 190 | 47% helix, 26% strand | P30793 |
| F, G | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 189 | 48% helix, 25% strand | P30793 |
| H, J | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 190 | 46% helix, 25% strand | P30793 |
| N | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 190 | 47% helix, 26% strand | P30793 |
| R | GTP cyclohydrolase 1 (EC 3.5.4.16) | protein | 188 | 48% helix, 24% strand | P30793 |
| a, c, e, g, h, j, k, m, o, q, r, t | GTP cyclohydrolase 1 feedback regulatory protein | protein | 84 | 19% helix, 43% strand | P30047 |
| b | GTP cyclohydrolase 1 feedback regulatory protein | protein | 83 | 19% helix, 43% strand | P30047 |
| d, f, i, l, n, p, s | GTP cyclohydrolase 1 feedback regulatory protein | protein | 83 | 19% helix, 41% strand | P30047 |
Ligands and binding sites
- QBQ · 7-deaza-GTP · ligand · 20 copies · chains A, E, F, B, J, C, I, D, H, G, K, O, P, L, T, M, S, N, R, Q
- PHE · Phenylalanine · ligand · 20 copies · chains B, a, b, C, c, D, d, E, e, A, F, f, j, G, g, H, h, I, i, J, L, k, l, M, m, N, n, O, o, K, Q, p, q, R, r, S, s, T, t, P
- 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 | 1101 | 0.89 | 0.91 | 123 | PHE |
| 2 | 1127 | 0.89 | 0.90 | 135 | PHE |
| 3 | 1039 | 0.89 | 0.90 | 117 | PHE |
| 4 | 796 | 0.87 | 0.90 | 96 | PHE |
| 5 | 273 | 0.78 | 0.91 | 48 | PHE |
Interfaces
119 interfaces between chains.
- O–P · 2023 Ų buried · 22 hydrogen bonds · protein-protein
- K–T · 2014 Ų buried · 23 hydrogen bonds · protein-protein
- A–J · 2006 Ų buried · 21 hydrogen bonds · protein-protein
- E–F · 2001 Ų buried · 18 hydrogen bonds · protein-protein
- N–Q · 1996 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 7ALB · human GCH-GFRP stimulatory complex 7-deaza-GTP bound · 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
- Every structure of UniProt P30047
- Elsewhere: RCSB PDB 7ALB · PDBe 7ALB · UniProt P30793 · UniProt P30047
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