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The 1.25 a resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from mycobacterium tuberculosis, crystal form II
Analyse The 1.25 a resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C90
- Type
- protein
- Length
- 348 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosyl-ATP pyrophosphatase
- EC
- 3.6.1.31
- UniProt
- P0A5B1
Structure
x-ray diffraction · 1 distinct chain · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X, A, B, C | Phosphoribosyl-ATP pyrophosphatase (EC 3.6.1.31) | protein | 87 | 80% helix, 0% strand | P0A5B1 |
Interfaces
3 interfaces between chains.
- B–C · 2000 Ų buried · 20 hydrogen bonds · protein-protein
- X–A · 1985 Ų buried · 26 hydrogen bonds · protein-protein
- X–B · 89 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3C90 · The 1.25 A Resolution Structure of Phosphoribosyl-ATP Pyrophosphohydrolase from… · the same entry in another collection · chain X against X, 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 P0A5B1
- Elsewhere: RCSB PDB 3C90 · PDBe 3C90 · UniProt P0A5B1
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