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Crystal structure of human guanosine monophosphate reductase 2 GMPR2 in complex with imp
Analyse Crystal structure of human guanosine monophosphate reductase 2 GMPR2 in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BZN
- Type
- protein
- Length
- 2,548 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gmp reductase 2
- EC
- 1.7.1.7
- UniProt
- Q9P2T1
- Ligands
- IMP
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 5 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, H | Gmp reductase 2 (EC 1.7.1.7) | protein | 320 | 36% helix, 23% strand | Q9P2T1 |
| B, G | Gmp reductase 2 (EC 1.7.1.7) | protein | 317 | 38% helix, 24% strand | Q9P2T1 |
| C | Gmp reductase 2 (EC 1.7.1.7) | protein | 317 | 39% helix, 24% strand | Q9P2T1 |
| D | Gmp reductase 2 (EC 1.7.1.7) | protein | 316 | 37% helix, 24% strand | Q9P2T1 |
| F | Gmp reductase 2 (EC 1.7.1.7) | protein | 321 | 38% helix, 23% strand | Q9P2T1 |
Ligands and binding sites
- IMP · Inosinic acid · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 682 | 0.78 | 0.83 | 62 | IMP |
| 2 | 696 | 0.78 | 0.83 | 60 | IMP |
| 3 | 697 | 0.77 | 0.82 | 62 | IMP |
| 4 | 688 | 0.77 | 0.82 | 72 | IMP |
| 5 | 566 | 0.77 | 0.83 | 63 | IMP |
Interfaces
16 interfaces between chains.
- E–F · 1149 Ų buried · 19 hydrogen bonds · protein-protein
- G–H · 1104 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 1072 Ų buried · 20 hydrogen bonds · protein-protein
- A–C · 1067 Ų buried · 20 hydrogen bonds · protein-protein
- E–G · 1060 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 2BZN · Crystal structure of human guanosine monophosphate reductase 2 GMPR2 in complex with IMP · the same entry in another collection · chain H against H, TM-score 1.00
- Q9P2T1 · AlphaFold monomer V2.0 prediction for gmp reductase 2 (Q9P2T1) · a predicted model of the same protein · chain B 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 Q9P2T1
- Elsewhere: RCSB PDB 2BZN · PDBe 2BZN · UniProt Q9P2T1
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