Research workbench
Structure of human guanosine monophosphate reductase GMPR1 in complex with gmp
Analyse Structure of human guanosine monophosphate reductase GMPR1 in complex with gmp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BLE
- Type
- protein
- Length
- 337 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gmp reductase I
- EC
- 1.7.1.7
- UniProt
- P36959
- Ligands
- 5GP, NA
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gmp reductase I (EC 1.7.1.7) | protein | 337 | 38% helix, 19% strand | P36959 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 213 | 0.80 | 0.94 | 43 | 5GP |
Compared structures
- 2BLE · Structure of human guanosine monophosphate reductase GMPR1 in complex with GMP · the same entry in another collection · chain A against A, TM-score 1.00
- P36959 · AlphaFold monomer V2.0 prediction for gmp reductase 1 (P36959) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P36959
- Elsewhere: RCSB PDB 2BLE · PDBe 2BLE · UniProt P36959
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