MolNFT v1 · #173966 · protein
Crystal structure of MTHISN2-AMP complex, a bifunctional enzyme from the histidine biosynthetic pathway
7BGN · Phosphoribosyl-AMP cyclohydrolase: “Crystal structure of MTHISN2-AMP complex, a bifunctional enzyme from the histidine biosynthetic pathway”. X-ray diffraction, 3 ligands (AMP, ZN, MG), 20 pockets (best druggability 0.79). MolNFT v1…
- PDB
- 7BGN
- Type
- protein
- Length
- 1,229 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosyl-AMP cyclohydrolase
- EC
- 3.5.4.19, 3.6.1.31
- UniProt
- A0A072U2X9
- Ligands
- AMP, ZN, MG
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 6 distinct chains · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19, 3.6.1.31) | protein | 204 | 43% helix, 22% strand | A0A072U2X9 |
| B | Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19, 3.6.1.31) | protein | 205 | 45% helix, 21% strand | A0A072U2X9 |
| C | Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19, 3.6.1.31) | protein | 204 | 43% helix, 21% strand | A0A072U2X9 |
| D | Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19, 3.6.1.31) | protein | 203 | 44% helix, 22% strand | A0A072U2X9 |
| E | Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19, 3.6.1.31) | protein | 202 | 44% helix, 22% strand | A0A072U2X9 |
| F | Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19, 3.6.1.31) | protein | 211 | 45% helix, 21% strand | A0A072U2X9 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · 11 copies · chains A, B, C, D, E, F
- ZN · Zinc ion · metal · 18 copies · chains A, B, C, D, E, F
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 2 copies · chains D, 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, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1023 | 0.79 | 0.81 | 76 | AMP, ZN |
| 2 | 1149 | 0.78 | 0.80 | 101 | AMP |
| 3 | 175 | 0.61 | 0.83 | 36 | empty |
| 4 | 230 | 0.60 | 0.80 | 38 | empty |
| 5 | 190 | 0.60 | 0.82 | 35 | empty |
Interfaces
9 interfaces between chains.
- A–B · 3925 Ų buried · 47 hydrogen bonds · protein-protein
- C–D · 3894 Ų buried · 45 hydrogen bonds · protein-protein
- E–F · 3886 Ų buried · 45 hydrogen bonds · protein-protein
- C–E · 323 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 272 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7BGN · Crystal structure of MtHISN2-AMP complex, a bifunctional enzyme from the histidine… · the same entry in another collection · chain A against A, 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 A0A072U2X9
- Elsewhere: RCSB PDB 7BGN · PDBe 7BGN · UniProt A0A072U2X9
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