Research workbench
1.45 a resolution of sporosarcina pasteurii urease inhibited in the presence of nbpto
Analyse 1.45 a resolution of sporosarcina pasteurii urease inhibited in the presence of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H8J
- Type
- protein
- Length
- 792 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Urease subunit gamma; Urease subunit beta; Urease subunit alpha
- EC
- 3.5.1.5
- UniProt
- A0A0H3YGY5, P41021, A0A0H3YL32
- Ligands
- 2PA, NI, SO4
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 3 distinct chains · 30% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Urease subunit gamma (EC 3.5.1.5) | protein | 100 | 56% helix, 18% strand | A0A0H3YGY5 |
| B | Urease subunit beta (EC 3.5.1.5) | protein | 122 | 15% helix, 31% strand | P41021 |
| C | Urease subunit alpha (EC 3.5.1.5) | protein | 570 | 29% helix, 22% strand | A0A0H3YL32 |
Ligands and binding sites
- 2PA · Diamidophosphate · ligand · chains C
- NI · Nickel (II) ion · metal · 2 copies · chains C
- SO4 · Sulfate ion · ion · 5 copies · chains A, C, B
- EDO · 1,2-ethanediol · additive · 13 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 830 | 0.72 | 0.77 | 90 | EDO |
| 2 | 102 | 0.36 | 0.74 | 17 | EDO |
Interfaces
3 interfaces between chains.
- B–C · 1865 Ų buried · 36 hydrogen bonds · protein-protein
- A–C · 927 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 223 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent, 2 modified (additive adduct, carboxylation).
Compared structures
- 6H8J · 1.45 A resolution of Sporosarcina pasteurii urease inhibited in the presence of NBPTO · the same entry in another collection · chain A against A, TM-score 1.00
- P41021 · AlphaFold monomer V2.0 prediction for urease subunit beta (P41021) · a predicted model of the same protein · chain B 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 A0A0H3YGY5
- Every structure of UniProt P41021
- Every structure of UniProt A0A0H3YL32
- Elsewhere: RCSB PDB 6H8J · PDBe 6H8J · UniProt A0A0H3YGY5 · UniProt P41021 · UniProt A0A0H3YL32
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