Research workbench
Crystal structure of methanobacterium thermoautotrophicum phosphoribosyl-AMP cyclohydrolase hisi
Analyse Crystal structure of methanobacterium thermoautotrophicum phosphoribosyl-AMP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZPS
- Type
- protein
- Length
- 252 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphoribosyl-AMP cyclohydrolase
- EC
- 3.5.4.19
- UniProt
- O26347
- Ligands
- CD
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) | protein | 124 | 10% helix, 40% strand | O26347 |
| B | Phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) | protein | 128 | 13% helix, 43% strand | O26347 |
Ligands and binding sites
- CD · Cadmium ion · metal · 19 copies · chains A, B
- ACY · Acetic acid · additive · 5 copies · chains A, 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 280 | 0.60 | 0.79 | 34 | ACY, CD |
| 2 | 274 | 0.57 | 0.78 | 34 | CD |
Interfaces
1 interface between chains.
- A–B · 1621 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 1ZPS · Crystal structure of Methanobacterium thermoautotrophicum phosphoribosyl-AMP… · the same entry in another collection · chain A against A, TM-score 1.00
- O26347 · AlphaFold monomer V2.0 prediction for phosphoribosyl-AMP cyclohydrolase (O26347) · a predicted model of the same protein · chain A 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 O26347
- Elsewhere: RCSB PDB 1ZPS · PDBe 1ZPS · UniProt O26347
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