Research workbench
Structure of ohcu decarboxylase in complex with guanine
Analyse Structure of ohcu decarboxylase in complex with guanine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O74
- Type
- protein
- Length
- 992 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ohcu decarboxylase
- UniProt
- A1L259
- Ligands
- GUN
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 4 distinct chains · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ohcu decarboxylase | protein | 165 | 70% helix, 0% strand | A1L259 |
| B, D, E | Ohcu decarboxylase | protein | 164 | 71% helix, 0% strand | A1L259 |
| C | Ohcu decarboxylase | protein | 167 | 71% helix, 0% strand | A1L259 |
| F | Ohcu decarboxylase | protein | 168 | 70% helix, 0% strand | A1L259 |
Ligands and binding sites
- GUN · Guanine · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 776 | 0.73 | 0.78 | 88 | empty |
| 2 | 795 | 0.71 | 0.77 | 94 | empty |
| 3 | 473 | 0.66 | 0.78 | 59 | empty |
Interfaces
5 interfaces between chains.
- C–D · 1195 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 1194 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1191 Ų buried · 15 hydrogen bonds · protein-protein
- C–F · 389 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 204 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2O74 · Structure of OHCU decarboxylase in complex with guanine · the same entry in another collection · chain F against F, TM-score 1.00
- A1L259 · AlphaFold monomer V2.0 prediction for 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 A1L259
- Elsewhere: RCSB PDB 2O74 · PDBe 2O74 · UniProt A1L259
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