Research workbench
1.59 a resolution fluoride inhibited sporosarcina pasteurii urease
Analyse 1.59 a resolution fluoride inhibited sporosarcina pasteurii urease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CEX
- Type
- protein
- Length
- 792 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P41022, P41021, P41020
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 100 | — | P41022 |
| B | — | protein | 122 | — | P41021 |
| C | — | protein | 570 | — | P41020 |
Compared structures
- 4CEX · 1.59 A resolution Fluoride inhibited Sporosarcina pasteurii urease · the same entry in another collection · chain A against A, TM-score 1.00
- P41020 · AlphaFold monomer V2.0 prediction for urease subunit alpha (P41020) · a predicted model of the same protein · chain C against A, TM-score 0.99
- P41022 · AlphaFold monomer V2.0 prediction for urease subunit gamma (P41022) · a predicted model of the same protein · chain A against A, TM-score 0.99
- 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 P41022
- Every structure of UniProt P41021
- Every structure of UniProt P41020
- Elsewhere: RCSB PDB 4CEX · PDBe 4CEX · UniProt P41022 · UniProt P41021 · UniProt P41020
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